Peplife 2.0 - Browse by Modifications

This page lists the various Chemical modifications, N-terminal modifications as well as the C-terminal modifications that were incorportated in the anti-cancer peptides compiled in Peplife 2.0. For more information see User Guide.

Chemical Modifications

Modification Name	Total Entries
None	2561
NMe	8
Î±Me	2
2-aminobutyric acid (Abu)	2
N.A.	31
Reduced amide bonds Î¨(CH2NH)	32
Reduced carbamate Î¨(CH2OCONH)	16
Three N-linked carbohydrate chains	1
Five N-linked carbohydrate chains	1
Aib--Aminoisobutyric acid	7
5 kDa PEG at Cys at 39th position	1
20 kDa PEG at Cys at 39th position	1
30 kDa PEG at Cys at 39th position	1
40 kDa PEG at Cys at 39th position	1
tBu=tertiary butyl	1
PhG=phenylglycine	1
Aib=Î±-aminoisobutyric acid	1
Nle=norleucine	1
Nle=norleucine, O-Î²-glucosylated serine	2
Oct-octanoic moiety	1
PEGylation on Lys12	1
PEGylation	2
PEGylation on Lys21	1
Fatty acid ie n-octanoic acid present at serine at position 3, (125)I labelling	1
Biotinylation at Lys at 34th position	4
Biotinylation at Lys at 34th and 26th position	4
Agp=Î±amino-3-guanidino-propionic acid	4
Dpr-2,3-Diaminopropionic acid	1
Glp-Pyroglutamic acid	1
Gamma peptide linkage between the carboxyl group of the glutamate side-chain and the amine group of cysteine	1
2me-2-methyl(tryptophan)	4
4-aminobutyric acid (Aba)	1
Pegylation at Lysine	2
Pen=Penicillamine, Methylation at Tyrosine, Tic=tetrahydroisoquinoline carboxylic acid	1
Pegylation at N terminus His7	3
Pegylation on Lys34	3
X= structure given in paper	54
BIP	36
Dab =2,4-diamino-butyric acid	2
Nle	2
Radiolabelling of GLP-1by [123I]	2
Radiolabelling of exendin 3 at position 1 (histidine)	2
[ÏˆCH2-NH21-22]	1
Aib	1
2-hydroxy-1-(hydroxymethyl)	4
Methylation at phenylalanine	2
Nal, Pegylation	4
N-MeVal; N-methylvaline, EtPro; Ethylproline, N-MeThr; N-methylthreonine MePro; Methylproline, AMHA; 2-amino-5-methylhexanoic acid, N-MeLeu; N-methylleucine	3
Methylation on Arg7 and Tyr1	1
Methylation of nitrogen of amide bond b/w Glu1 and Leu2 (NMe); Methylation of carboxyl of Leu8	1
Methylation of nitrogen of amide bond b/w Glu1 and Leu2 (NMe)	1
Pyroglutamic acid	1
Methylation of carboxyl of Leu8	5
Methylation of carboxyl of Leu2 and Leu8	1
Methylation of carboxyl of Leu2	2
Methylation of carboxyl of Leu2 and amino-group of Thr9 used in peptide bond	1
Reduced bond between Leu8 and Thr9	1
Ornithine	1
Sar= sarcosine	1
Pegylation at K27	5
Pegylation at K20 and K28	1
Glycosylation at Thr-105	1
N₃-L-Hlys at 8th arginine position	3
N₃-1^d= COOH-CH(NH2)CH2-(CH2)3-CH2-NHMe at 8th arginine position	1
N₃-2= COOH-CH(NH2)CH2-(CH2)3-CH2-NMe₂at 8th arginine position	1
N₃-3= COOH-CH(NH2)CH2-(CH2)3-CH2-NMe₂at 8th arginine position	1
N₃-L-lys at 8th arginine position	1
N₃-4^d= COOH-CH(NH2)CH2-(CH2)3-CH2-NHMe at 8th arginine position	1
N₃-5^d= COOH-CH(NH2)CH2-(CH2)3-CH2-NMe₂ at 8th arginine position	1
N₃-6^d= COOH-CH(NH2)CH2-(CH2)3-CH2-⁺NMe₃ at 8th arginine position	1
N₃-L-Orn at 8th arginine position	1
N₃-7^d= COOH-CH(NH2)CH2-(CH2)3-CH2-⁺NHMe at 8th arginine position	1
N₃-8^d= COOH-CH(NH2)CH2-(CH2)3-CH2-Nme₂ at 8th arginine position	1
N₃-9^d= COOH-CH(NH2)CH2-(CH2)3-CH2-⁺Nme₃ at 8th arginine position	1
N₃-L-Arg at 8th arginine position	1
COOH-CH(NH2)-CH-CH-CH(NH)-C=NR(H2N) at 8th arginine position	1
COOH-CH(H2N)CH-CH-CH(HN)-CH(imidazole) at 8th arginine position	1
COOH-CH(NH2)CH-CH-CH(N-CH-CH-NH-C=NH-CH) at 8th arginine position	2
Conjugation of peptide C terminal carboxyl group with amino group of 5 Fluorocytosine	5
Thiomethylene bond replacement between residue 1-2	1
Thiomethylene bond replacement between residue 2-3	1
Thiomethylene bond replacement between residue 4-5	1
Thiomethylene bond replacement between residue 3-4	1
Tritium labeling at Proline	1
I125 radiolabeled	2
Sulphation of Tyrosine residue at position 2	2
Sulphation of Tyrosine residue at position 3	1
Sulphation of tyrosine residue at position 4	2
DAT-FPA was labeled with 125-iodine or with 123-iodine by chloramine-T	6
C14 Radiolabeling	27
pGlu = pyroglutamate	2
At 2 position cystine is replaced by cysteine	1
Peptide bonds at position 1,2 was replaced by thioamide linkages	1
Peptide bonds at position 2,3 was replaced by thioamide linkage	1
Para chlorination of amino group of phenylalanine	2
Para bromination of amino group of phenylalanine	2
Para florination of amino group of phenylalanine	2
Para iodination of amino group of phenylalanine	2
Hydroxylation of amino group of Phenylalanine	1
I125 radiolabeling and encapsulation of VIP in Liposome	2
I125 radiolabeling	12
Biotinylation at lysine residue(position 24)	1
Labelled with I125	1
pGlu=pyroglutamic acid, Tritium labeling	1
pGlu=pyroglutamic acid	10
Methylcarbamylated at serine (position 8)	1
Glycosylation	3
I125 labeling	41
Methylation of phenylalanine at 3rd position	6
Trp methylated at position 2	3
[2-dehydro-Pro1.5]C is attached and tritiated	1
The reduced bond psi [CH,-NH] was introduced at position 1-2	1
The reduced bond psi [CH,-NH] was introduced at position 3-4	1
The reduced bond psi [CH,-NH] was introduced at position 4-5	1
The reduced bond psi [CH,-NH] was introduced at position 5-6	1
The reduced bond psi [CH,-NH] was introduced at position 6-7	1
The reduced bond psi [CH,-NH] was introduced at position 7-8	1
The reduced bond psi [CH,-NH] was introduced at position 8-9	1
The reduced bond psi [CH,-NH] was introduced at position 9-10	1
Methylated at position 2 of D-trp	4
Î³-Glu-palmitoyl residue at position 21	9
Post translationaly modified Glu residue at first position	1
19 residue is N15 labelled, also have 13C carbon	1
Mal-PEG12-CP was conjugated to Cys-enfuvirtide	1
Ligated with potent cytotoxin thapsigargin, L12ADT	1
X = 6-aminohexanoic acid, B = beta-alanine, I = inosine	6
Tyr residue at 8 position is Iodionated	2
111In radiolabeling	1
pGlu=pyroglutamic acid, des-Gly	5
Î²Ala = Beta alanine	4
Ibu = Î±-aminoisobutyric acid	7
Î²Ala = Beta alanine, Orn = Ornithine	5
conjugated with cationic bovine serum albumin conjugated pegylated nanoparticles (CBSA-NPs), pGlu=pyroglutamic acid	1
I125 radiolabeling, covalently attached to an isocyanate-containing poly urethane prepolymer	2
Sar- Sarcosine	4
4th AA is D isoform of allo- Ile, Sar- Sarcosine	4
Sar- Sarcosine, Nva-Norvaline	1
Sar- Sarcosine , Nva-Norvaline	1
Sar- Sarcosine ,Nva-norvaline	1
Sar- Sarcosine , NMeNva- N-methyl-norvaline	3
conjugated with PEG	1
X1-Napthyl-alanine, X2-Sarcosine	10
Acpc=cyclopropylalanine	2
Pyr=pyroglutamic acid	2
(pF)F = p-flouro Phenylalanine; Aib= 2-Aminoisobutyric acid	2
Pyr-Glu= pyro-glutamate	1
4 Hexapeptide bound to PEG-Biotin to form tetra branched	1
n-octanoyl group at ser 3	2
Orn=Ornithine	6
Agp = Î±-amino-3-guanidinopropionic acid	2
Nir=Nitro-arginine	1
Nmr =N-methylarginine	1
Har=Homoarginine	2
D-Arg at 19th position	2
orn =Ornithine	1
Beta-Hr =Î²-homoarginine	1
D-Arg at 15th position	1
Har=Homoarginine, Agp = Î±-amino-3-guanidinopropionic acid	2
Har=homoarginine, Orn=Ornithine	1
Agp = Î±-amino-3-guanidinopropionic acid, Orn=Ornithine	1
D-Ala at 8th position	2
Î³-Glu-palmitoyl at 21 st position	3
X-1 = Cys- conjugated-7-hydroxyCoumarin maleimide	3
X-2 = Cys- conjugated-7-hydroxyCoumarin maleimide	3
X-2 = Lys- conjugated-7-hydroxyCoumarin maleimide	2
X-1 = Lys- conjugated-7-hydroxyCoumarin maleimide	1
Conjugated with PEG(40KDa) thro µgh Lys-30	2
Conjugated with ClPhSO2 conjugate thro µgh Lys-30	2
Conjugated with MorphSO2 conjugate thro µgh Lys-30	1
Acylation of peptide at K-26 with C-18(palmitic acid) fatty di-acid chain	2
Alpha-aminoisobutyric acid at 8th position, Acylation of peptide at K-26 with C-18 fatty di-acid chain	1
Acylation of peptide at K-26 with C-18 fatty di-acid chain	1
Pyro-Glutamate at 1st position	1
Lactose at N-ter, pyro-Glutamine at n-ter, D-Trp at 6 pos	2
Stearic acid at Lys	1
Succinimidyl 6-hydrazinonicotinate acetone hydrazone (HYNIC) derivatized, HYNIC conjugated at either at Cys -1 or Amine group Of Lys-2	1
Methylation of alpha-C of Pro	2
Modified Gly at 16th postion i.e. propargylglycine and peptide conjugated with drug DTX at this position	1
Pal=3-(2-Pyridyl)-L-alanine , k(Nic)=Nicotinoyl)Lys , Nle=NorLeucine, Dichloro at 5th Phenyl	1
Pyr=Pyro-glutamine	3
D-Nal =Napthylalanine	1
Cpa=Chlorophenylalanine	1
Iodinated at Tyr	3
Cyclo-Asp at 8th position, cyclo-Lys at 12 position	1
Pyr=Pyro-glutamic acid	2
Radioiodinated peptide at Tyr	6
Radioiodinated peptide at Tyr-4	2
pE=Pyro-glutamate, D-alanin= 3-(2Naphthyl)-D-alanine	2
4 nitro groups linked to Phenylalanine (phe) at 4th position	1
Labelled with 125I	1
Labelled with 125I, Disulphide bond is reduced	2
S-CM=S-carboxymethylated	1
pGlu= Pyro-glutamate	5
Tyr is Iodinated (125I)	9
D-Ser(tBu) at 6th position, Pglu=pyr- Glutamate	1
D-Ser(tBu) at 6th position	2
Peptide covalently attached to Isocyanate containing polyurethane prepolymer	3
Aib =2-Aminoisobutyric acid; Acylation of peptide at K-26 with fatty acid side chain i.e. N6-[N-(17-carboxy-1-oxoheptadecyl-L-c-glutamyl[2- (2-aminoethoxy)ethoxy]acetyl[2-(2 aminoethoxy)ethoxy]acetyl	2
Proline ring is tritiated	2
SO3H Group at Tyr-4, Coupled to PEG(10KDa), PEG=Polyethylene glycol, CCK-10=Cholecystokinin	2
Cu-labelled	2
pyr-Glu= Pyro-Glutamic acid	1
Npa-napthylalanine,Sar-sarcosine	25
Aib=Î±-aminoisobutyric acid replacing Ala8 and Gly35 of hGLP-1[7-36]	1
N-hydroxysuccinimide ester(NHS-ester)modified Cy5.5 at Lysine 15,23 and 27	1
N-hydroxysuccinimide ester(NHS-ester)modified Cy5.5 at Lysine 15,23 and 28	1
Pegylation-PEG750 of cysteine at 4th position	1
Pegylation-PEG2000 of cysteine at 4th position	1
Pegylation-PEG750 of cysteine at 11th position	1
Pegylation-PEG2000 of cysteine at 11th position	1
Pegylation-PEG750 of cysteine at 15th position	1
Pegylation-PEG2000 of cysteine at 15th position	1
Pegylation-PEG750 of cysteine at 18th position	1
Pegylation-PEG2000 of cysteine at 18th position	1
Pegylation-PEG750 of cysteine at 22nd position	1
Pegylation-PEG2000 of cysteine at22nd position	1
Pegylation-PEG750 of cysteine at 29th position	1
Pegylation-PEG2000 of cysteine at 29th position	1
Pegylation-PEG750 of cysteine at 20th position	1
Pegylation-PEG2000 of cysteine at 20th position	1
Iodination at tyr16	1
Glycosylation at 84thand 112th position	4
Glycosylation at 84th position	1
Azide-modified aptamer fragments (5 SSA and 3 SSA) "TTAATTCTGGGGGAGCCTTTTGTGGGTAGGGTTTTGTGGGTAGGGCGGGTTGGTTTTCGGGTTGGTTTTGCCCCGGAGGAGGAATT" are conjugated with DBCO-modified peptides (S10 and S11) , DBCO = Dibenzocyclooctyne	1
GLP-1 dimerization	3
Lys-30 is replaced by Arg and Lys-20 is acylated with a C16 palmitic acid linkd with γGlu	3
Lys8 conjugation with palmitoyl-Glu(2)-OH	8
Humanized anti-HER2 scFv P1h3, albumin-binding peptides (ABD035 or dAb7h8), cathepsin B-cleavable peptide B2, endosome-disruptive peptide E5C3 fusion protein, GN= Gasdermin-N	3
R= OH for Cys35	8
Ahx links two peptide	1
A palmitoyl group is conjugated to DR10627 via a -γ-glutamyl-linker connected to the Lys10 position	3
Alkyl chain conjugated with Lys2 side chain	1
Alkyl chain conjugated with Lys2, Lys4 side chain	1
At position 10 of the peptide sequence, modifications involving octadecanedioic acid (C18) and a glycine/serine-based linker "GGSGSG" were introduced, Aib modification,D-serine	4
Aib modification at position 2, Lys20 side chain conjugated with (ADO-linker-Glu-C18)	3
C20 fatty diacid moiety conjugated with Lys20, Aib modification at position 2,13	1
Radiolabelled with technetium, X= Unknown Structure	1
palm-Glu-OH conjugated at Lys9 side chain	1
D-Tryp amino acid substituition, d-Dab = Diaminobutyric acid	1
C41H70O15N4 fatty acid modification	1
Aib2, aMeF(2F)6, 4PallO, aMeL13, Ornl6, K17, Aib20, D-Glu24 aMeY25, and Ser39 substituitions, Lys17 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)16-CO2H)	6
Aib2, aMeF(2F)6, aMeL13, Ornl6, K17, Aib20, D-Glu24, and Ser39 substituitions, Lys17 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)16-CO2H)	2
Aib2, Aibl3 and 1-Nal22 substituitions, Lys20 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)18-CO2H)	3
Aib2, Aibl3 substituitions, Lys20 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)1-CO-(CH2)18-CO2H)	3
V24L modifications	39
Mn and 89Zr labeling, MNPs modified with WL12-SH	2
Incorporation of 4-thiaproline (Thp) at position cisPro76	1
Alanine (Ala) is substituted with valine (Val) at position 81	2
leucine (Leu) is substituted with proline (Pro) at position 55	1
Conjugate in which LYS27 side chain linked to PEG-Fc	13
Aib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18(3H)	1
Aib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18(3H), other metabolite may be attached	2
Aib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)	42
L98R and P171A amino acid substitutions in FBGF21	1
Biotinylation	6
Cy7	2
IL-7Ra binding domain linked with yc binding domain with the help of linker GGS linker	2
fluorescently labeled with Atto647N, polysarcosine-block-poly(S-ethylsulfonyl-l-cysteine)	3
Removing an Asp residue	1
Lys33 conjuagted with HLE (fatty acid based half life extension group),Substituting Ser with 2-aminoisobutyric acid (Aib) at position 2	1
E16, K20 modification	1
C‐mannosylated tryptophan residue at position 8	1
α-(4-pentenyl)-Ala introduced at positions 3 of DR8	1
α-(4-pentenyl)-Ala introduced at positions 4 of DR8	1
Addition of a C16 monoacid at position 20 of the hGLP-2 peptide	1
Orn=Ornithine at position 15	5
Orn at postion 19	8
Fluorescently labeled	13
X=Structure given in paper	3
Aib = α-aminoisobutyric acid	18
Aib = α-aminoisobutyric acid, Iva = Isovaline	4
X = Octanoyl-Dpr at position 3	9
X = Octanoyl-Dpr at position 3, NMeS = N-Methyl-L-Serine at position 2	1
X = Octanoyl-Dpr at position 3, Deg = Di-ethyl glycine at position 2	1
X = Octanoyl-Dpr at position 3, Tie = L-te/t-butyl-glycine at position 2	1
X = Octanoyl-Dpr at position 3, Aib = 2-aminoisobutyric acid at position 2	1
X = Octanoyl-Dpr at position 3, NMeS = N- methyl-L-serine at position 2	1
X = Octanoyl-Dpr at position 2	1
X = Octanoyl-Dpr at position 3, 1Nal = 3-(l-naphthyl)-L-alanine at position 4	1
NMeS = N- methyl-L-serineat position 2,X = Octanoyl-Dpr at position 3, Nal = 3-(l-naphthyl)-L-alanine at position 4	1
Aib at position 2, Chem. 8 [2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33	2
Aib at position 2, Chem. 7 [(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(17-carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys33	1
Aib at position 2, Chem. 7 [(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(17- carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys16	2
Aib at position 2 and 13, Chem.16[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(19- carboxynonadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys	1
Aib at position 4, Chem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33	2
Aib at position 4,Chem. 10[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4- carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys33	1
Aib at position 4,Chem. 7[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(17-carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys 16	1
Aib at position 4,Chem. 11[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(19-carboxynonadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys20	1
Chem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33 , Sar2, Aib modifications	1
Aeg = N-(2-aminoethyl)glycine, Chem.16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Aeg2, Chem.8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy]acetyl] attached to Lys33	1
Chem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33, Sar2 modification	1
Chem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33	1
Chem. 10[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4- carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys33, Sar2 modfications	1
Chem. 10[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4- carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys33, Sar2 modifications	1
Chem. 10[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys33, Sar2 modifications	1
Chem. 7[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4- carboxy-4-(17-carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys33, Sar2 modifications	1
Chem. 7[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(17- carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys 16, Sar2 modifications	1
Chem.7[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(17- carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys16, Aib modifications	1
Chem.11 [2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(19- carboxynonadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys20, Sar2 modification	1
Aib at position 2, Chem. 10[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl attached to Lys33	1
Chem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33 , Sar2 modification	1
Chem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33, Sar2 modifications	2
Chem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4- carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33	1
Aib2 modification	6
D-Ser2 substiuition, Lys14 side chain linked to C16 fatty acid via linker yE-C16	1
D-Ser2 substiuition	1
Lys20 side chain linked to C16 fatty acid via linker yE-C16	1
Liver-targeting glycosylation signature conjugated to a deaminated gliadin peptide	1
Aib, GC15136 and HMC001 are linked via a 10-kDa, bifunctional maleimide-polyethylene glycol-aldehyde (MAL-PEG-ALD) linker	6
all Proline radiolabelled with [3H]	1
w=D-Trp,Mesityl	5
d-Leucine6 substituitions	2
Ole = oleic acid conjugation	1
Cysteine was introduced at position 10	3
Cysteine was introduced in the sequence of both peptides at position 10	3
Cys10 replaced by Ser10	1
Carbamidomethylation of Cys10 residue = Cdm	1
Cys replaced by Ser	3
Carbamidomethylation of Cys residue = Cdm	3
125I labeled	5
Attachment of a lipid moiety (C18-γ-Glu-PEG2) at K25 position, Aib, Nle,acetylation of Lys10	1
Attachment of a lipid moiety (C18-γ-Glu-PEG2) at K34 position, Aib, Nle	1
Modified at position 2 with an aza-amino acid (aza-proline)	1
Modified at position 3 with an aza-amino acid (aza-proline)	1
Modified at position 4 with an aza-amino acid (aza-glycine)	1
Modified at position 5 with an aza-amino acid (aza-phenylalanine)	1
Modified at position 7 with an aza-amino acid (aza-proline)	1
Modified at position 8 with an aza-amino acid (aza-phenylalanine)	1
Modified at position 9 with an aza-amino acid (aza-arginine)	1
Modified at both positions 2 and 8 with aza-amino acids (aza-proline and aza-phenylalanine, respectively)	1
Modified at both positions 5 and 8 with aza-amino acids (aza-phenylalanine)	1
Glucosylation at Asn15	2
Glucosylation at Asn26	2
Glucosylation at Asn34	2
N-glycosylation with biantennary complex-type N-glycan at Asn15 (G2 glycoform = glycan)	2
N-glycosylation with sialylated biantennary complex-type N-glycan at Asn15 (G2S2 glycoform = sialylated glycan)	2
N-glycosylation with biantennary complex-type N-glycan at Asn26 (G2 glycoform = glycan)	2
N-glycosylation with sialylated biantennary complex-type N-glycan at Asn26 (G2S2 glycoform = sialylated glycan)	1
N-glycosylation with sialylated biantennary complex-type N-glycan at Asn26(G2S2 glycoform = sialylated glycan)	1
N-glycosylation with biantennary complex-type N-glycan at Asn34 (G2 glycoform = glycan)	2
N-glycosylation with sialylated biantennary complex-type N-glycan at Asn34 (G2S2 glycoform = sialylated glycan)	2
Native oxytocin peptide was modified with a substitution of the Leu8 to a Lys appended with a polyethylene glycol space and a palmitoyl group and with a substitution of Gly for the Pro7	3
D-amino acid residue (D-Lys) inserted at position 2	4
Cy5 conjugation	6
cyclised on TATA (1,3,5-Triacryloylhexahydro-1,3,5-triazine), 1Nal - 3-(1-naphthyl)-L-alanine, HArg – homo-arginine, HyP – hydroxyproline, MMAE = Monomethyl auristatin E, Cys16 with amidation modification, D-Asp4 modification	11
Modified by adding negative charge	2
Dmt: 2',6'-dimethyltyrosine	1
Dmt: 2',6'-dimethyltyrosine at position 3, D-Arg2 modification	1
DiR labeled	1
X = R1, R2 = H (R2 group present in R1)	5
X = R1, R2 = H (R2 group present in R1), Y = R3, R4 = Zr (R4 group present within R3)	7
Albumin binding fatty-acid side chain is coupled to lysine (B29)	4
177Lu radiolabeling at PEG4, Lys1 and Glu2 linked with PEG4 in between	4
177Lu radiolabeling at PEG4	4
Gln 6,14 modification, Mod = (CH3)2CHSO2-, N3-linker N-hydroxysuccinymidocarbonates containing isopropyl sulfone (1A) and N,N-dimethyl-sulfonamide (1B) modulators	1
Gln 6,14 modification, Mod = (CH3)2CHSO2-, N3-linker N-hydroxysuccinymidocarbonates containing N,N-dimethyl-sulfonamide (1B) modulators	1
Gln 6,14 modification, Mod = (CH3)2CHSO2-	1
Gln 6,14 modification, Mod = (CH3)2NSO2-	1
Replacing the isoleucine (Ile7) residue with D-alanine7 (D-Ala)	1
C16-diacid acylation at Lysine16	1
Insertion of a cysteine residue at position 31 for pegylation PEG20 acetamide	1
Insertion of a cysteine residue at position 31 for pegylation	1
PEG10K-MAL fatty chain-modification of rhG-CSF at Cys18 position	1
C15-MAL fatty chain-modification of rhG-CSF at Cys18 position	1
C20 fatty diacid conjugation at the side chain of the Lys20, Aib = alpha-amino isobutyric acid at position 2,13	4
D serine modifcation at 2, side chain modification at Lysine (n=12, R=CH3)	6
D-leucine at position 1 and 3	1
introduction of Cha = cyclohexylalanine residues at position 7,E1A substituitions	1
introduction of Cha = cyclohexylalanine residues at position 7	1
introduction of Cha residues at positions 7 and 12	2
Conjugation of TT1 and IP proteins which is linked by Ahx	2
An ester bond is utilized to attach Dox with a glutaryl linker	1
1 Fatty acid conjugation through pAzF (para-azidophenylalanine)	2
5 Fatty acid conjugation through pAzF (para-azidophenylalanine)	2
10 Fatty acid conjugation through pAzF (para-azidophenylalanine)	2
Agp	3
Phe linked with (2-Cbm),3Pal, Orn linked with iPr	5
e=D-Glutamic acid, r=D-Aspartic acid, k=D-Lys, Cy5 = indocarbocyanine dye conjugated with Lys at C terminal, X=linker	1
e=D-Glutamic acid, r=D-Aspartic acid, k=D-Lys, Alb=albumin, Cy5 = indocarbocyanine dye conjugated with Lys at C terminal, X=linker	1
e=D-Glutamic acid, r=D-Aspartic acid, k=D-Lys, Dex=Dextran, Cy5 = indocarbocyanine dye conjugated with Lys at C terminal, X=linker	1
e=D-Glutamic acid, r=D-Aspartic acid, k=D-Lys, Strep=Streptavidin, Cy5 = indocarbocyanine dye conjugated with Lys at C terminal, X=linker	2
Aib substituitions at position 2 of semaglutide	1
A22K(N(eps)tetradecanedioyl-4×gGlu), B3E, B26E modification, A and B chain linked with disulfide bond	1
A22K(N(eps)tetradecanedioyl-gGlu-2×OEG), B3E, B27E, B28E modifications, , A and B chain linked with disulfide bond	1
A22K(N(eps)tetradecanedioyl-gGlu-2×OEG), B3E, B28D modifications, A and B chain linked with disulfide bond	1
A22K(N(eps)tetradecanedioyl-4×gGlu), B3E, B28D modifications, A and B chain linked with disulfide bond	1
A22K(N(eps)hexadecanedioyl-4×gGlu-2×OEG), B3E, B26E modifications	6
A14E, A22K(N(eps)tetradecanedioyl-4×gGlu), B3E, B27E, B28E modifications, A and B chain linked with disulfide bond	1
A22K(N(eps)tetradecanedioyl-4×gGlu), B3E, B28D modification, A and B chain linked with disulfide bond	1
A22K(N(eps)tetradecanedioyl-4×gGlu), B3E, B26E, B28E modificatino, A and B chain linked with disulfide bond	1
A22K(N(eps)tetradecanedioyl-4×gGlu), B3E, B26E modifications, A and B chain linked with disulfide bond	1
A22K(N(eps)tetradecanedioyl-gGlu-2×OEG) modifications	1
A22K(N(eps)tetradecanedioyl-4×gGlu), B28D modifications	1
A22K(N(eps)hexadecanedioyl-gGlu-2×OEG), B3E, B28D modifications, A and B chain linked with disulfide bond	1
A22K(N(eps)hexadecanedioyl-gGlu-2×OEG), B3E, B27E, B28E modifications, A and B chain linked with disulfide bond	1
A22K(N(eps)hexadecanedioyl-4×gGlu), B3E, B26E modifications, A and B chain linked with disulfide bond	1
A22K(N(eps)hexadecanedioyl-gGlu-2×OEG), B3E, B26E modifications, A and B chain linked with disulfide bond	1
A22K(N(eps)hexadecanedioyl-gGlu-2×OEG) modification	1
Mod = (CH3)2CHSO2-MS-BCN microsphere conjugation	2
Mod = (CH3)2NSO2-MS-BCN microsphere conjugation	2
additional modification (Asp residue)	1
Residue Glu187 of the Ca1 site in the catalytic domain was replaced by Ala	1
D-Leu, D-ala = l and a, Proline side chain linked with (4Br-Phe) at C terminus	1
D-Arg = r, D-Gln = q, D-Leu = l, D-ala = a, Proline side chain linked with (4Br-Phe) at C terminus	1
I125 radioactive labeled	1
C7-C7 and C20-C19 disulfide bond between A and B chain	28
Conjugating a myristic acid-acylated lysine to a permissive site of TP5, Radiolabeling C14 at Lys2	2
Conjugated to a C20 fatty diacid moiety via a linker connected to the lysine residue at position 20 (C20 diacid-yGlu-(AEEA)2), two non-coded amino acid residues at positions 2 and 13 (Aib, α-amino isobutyric acid)	6
C20 fatty diacid moiety at Lys20	3
Methylated Gln34	1
Methylated Arg33	1
β-homoGln34 modification	1
β-homoArg33 modification	1
Trp30 modification, Methylated Arg35	1
Trp30 modification	1
hle5 = D-homoleucine, Pff6 = Phe(4-F), Orn = Ornithine,Replaces the C-terminal Arg of PMX53 with a hydrophobic amino acid	1
cha4 = D-cyclohexylalanine, O2 = Ornithine	1
Fatty acid conjugation at position 4 (C18 diacid-γGlu-2xAdo)	1
Fatty acid conjugation at position 5	1
Fatty acid conjugation at position 9	1
Fatty acid conjugation at position 10	1
Fatty acid conjugation at position 11	1
Fatty acid conjugation at position 13	1
Fatty acid conjugation at position 22	1
Fatty acid conjugation at position 23	1
Fatty acid conjugation at position 29	1
Fatty acid conjugation at position 30	15
Fatty acid conjugation at position 33	1
Fatty acid conjugation at position 35	1
Fatty acid conjugation at position 4, MeArg4	1
Fatty acid conjugation at position 30, Acetylation at Asn28	4
Mal links KKK and other peptide	1
D-Cha3: cyclohexylalanine	3
Substitution of L-serine at position 2 with α-aminoisobutyric acid (Aib), X1 = Structure given in paper	1
FLAG tag	2
FITC labeled	4
All Alanine replaced by β-alanine	1
Fab conjugation, Lys1 fatty acid conjugation (Palm)	1
AF488 labeled , Lys1 fatty acid conjugation (Palm)	1
M, R amino acid substitutions	1
Substituition of A with Y at position 10	3
LPPTNVGSNTP all D-amino acids, Lipidation on Lys1	1
GDM linker with a two-carbon spacer between the β-carbon and the triazole, Mod = NC−, X = Structure given in paper (n=0)	3
GDM linker with a three-carbon spacer between the β-carbon and the triazole, Mod = PhSO2−, X = Structure given in paper (n=1)	3
GDM linker with a four-carbon spacer between the β-carbon and the triazole, Mod = MeSO2−, X = Structure given in paper (n=2)	2
DOTA-LM3 conjugation, Cbm = Carbamoyl, 177Lu labeling, pCl-Phe = P-Chloro Phenyalanine	4
Substituition of amino acid G at position 2	2
Substituition of amino acid A at position 2	2
Poly(L-glutamic acid) is grafted with methoxy poly(ethylene glycol) (PEG) using a pH-sensitive linker, 2-propionic-3-methylmaleic anhydride = CDM	1
Poly(L-glutamic acid) is grafted with methoxy poly(ethylene glycol) (PEG) using a pH-sensitive linker, CDM = 2-propionic-3-methylmaleic anhydride	1
PEGylation through an MMP-sensitive peptide linker (PLGLAG), CDM = 2-propionic-3-methylmaleic anhydride	1
Arg8-Arg9 was replaced by a reduced amine bond (Ψ[CH2NH]) between Lys8-Lys9	2
Pro10 was then substituted by the silylated proline analog silaproline(Sip) , Arg8-Arg9 was replaced by a reduced amine bond (Ψ[CH2NH]) between Lys8-Lys9	1
Di-substitution with both Sip and TMSAla, Arg8-Arg9 was replaced by a reduced amine bond (Ψ[CH2NH]) between Lys8-Lys9	1
Lys24 conjugated with(-(γE)3-C16), Aib	1
Lys24 conjugated with (-(γE)3-C16), PEGylation,Aib,Nle	2
Lys24 conjugated with (-(γE)3-C18), PEGylation,Aib,Nle	1
Lys24 conjugated with (-(γE)3-C18), PEGylation,Aib,Nle,acetylation at Lys10 and Lys23	3
Lys24 conjugated with (-(PEG2)3-(γE)3-C16), PEGylation,Aib,Nle,acetylation at Lys10 and Lys23	1
Lys24 conjugated with (-(PEG2)3-(γE)3-C18), PEGylation,Aib,Nle,acetylation at Lys10 and Lys23	1
Lys24 conjugated with (-(PEG2)3-(γE)3-C16-OH), PEGylation,Aib,Nle,acetylation at Lys10 and Lys23	1
Lys24 conjugated with (-(PEG2)3-(γE)3-C18-OH), PEGylation,Aib,Nle,acetylation at Lys10 and Lys23	1
Serine, threonine and glycine were added to the linker	1
replacing L-Arg15,19 with D-Arg15,19	4
GLP-1 linked with GA3 through L3 linker, FITC labeled	1
GLP-1 linked with ABD035 through L3 linker, amino acid subsituitions with F,R,K,E,K,L,H, FITC labeled	1
GLP-1 linked with ABDCon through L3 linker, amino acid subsituitions with K,E,K,I,E,K,I,T,F,D,K,N,K,K, FITC labeled	1
Conventional unsubstituted β-eliminative linker, linked by a GDM linker and Mod = (CH3)2NSO2−	1
Conventional unsubstituted β-eliminative linker	2
with GDM linker and Mod = (CH3)2NSO2−	1
Three amino acid residues (GAP) from the FVIII/XTEN junction and 9 amino acids (PPVLKRHQA) from the FVIII B-domain linker were removed, LVPR thrombin site located between DʹD3 and Fc on constructs 1 and 2 was replaced with an FVIII acidic region 2 (a2) thrombin site	10
2-(7-octenyl)alanine-2-(4-pentenyl)alanine modifications	1
Uncarboxylation at all glutamic acid	2
O-glycosylation likely at Ser8 in SVPSPDP, Uncarboxylation at all glutamic acid	2
Aib substiuition at position 2, Ser39 linked with fatty acid	1
Aib substiuition at position 2,Ser39 linked with fatty acid	1
C1 = structure given in paper, Aib substiuition at position 2,Ser39 linked with fatty acid	1
C1 = structure given in paper,Aib substiuition at position 2,Ser39 linked with fatty acid	1
Modification of 6a and 6b with the introduction of C2 = structure given in paper,Aib substiuition at position 2,Ser39 linked with fatty acid	2
Small set of mutations, including His2, Lys24, and P29	2
Lipidation	16
hArg = Homo-Arginine, NMeLeu, Oic = Unnatural amino acid	11
hArg = Homo-Arginine, NMeLeu, Oic = Unnatural amino acid	2
Blue fluorescent protein (BFP) labeling	1
Cysteine substiution at 10, 17	2
Cysteine substiution at 23, 30	2
Modifcation of lysine site at position at 16 with C16 fatty acid	3
Conjugation of palmitic acid at AzF, biotinylated labelling, , (AzF) was incorporated into the position 126 on the repebody followed by lipid conjugation	1
TAMRA labeled	1
Sip amino acid substiution	2
Sip amino acid substiution, TMSAla substuition	2
Substiution of Y amino acid with K	4
Substiution of Y amino acid with d-W	2
Substiution of Y, I amino acid with Dmt, Tle	1
Substiution of Y, I amino acid with Dmt	1
3H labeling at proline5 residue	3
PEGylation at Asn637 in native gp41	1
Radioiodinated , A8G, G31C modification in GLP-1	3
Modifications include (R-octenyl alanine) and (Bis-pentenyl glycine)	1
Modifications include (S-octenyl alanine) and (Bis-pentenyl glycine)	1
Modifcations include (R-octenyl alanine) and (bis-pentenyl glycine) and (S-octenyl alanine)	1
Incorporation of HSA at V16 of GLP_1C	1
Incorporation of HSA at Y19 of GLP_1C	1
Incorporation of HSA at F28 of GLP_1C	1
Incorporation of D-ser in place of L-ser at 2nd position	1
Two cysteine group conatins fatty acid moteity(L3 = Structure given in paper) , Incorporation of D-ser in place of L-ser at 2nd position	1
(X1) MPAs modification on Lys12	3
(X2) MPAs modification on Lys12	3
(X3) MPAs modification on Lys12	3
Single atom O toS substitution (X=S)	1
G,E,T,S,L,A,A,A,A amino acid substuitions at positions 2,3,5,8,10,11,16,24,28 respectively	1
G amino acid substituition at position 2	6
Gly2, Nle10, D-Phe11, Leu16 modification	8
VH and VL joined by linker (GGGGS)3	1
ICP NPs were stacked into nanoparticle clusters upon coating with DA modified HA, Folic acid	1
Replaces 18A with a modified central region of apoC-II	2
PEGylation at His2	4
Amino acid residues located at 24 substituted by the residues of Exenatide in the same location, Position 16 was replaced by Cys for coupling hybrid peptides with fatty chains	1
Gln28 modifcations	4
HomoArg6 replaces Arg (R)	1
4GuanPhe6 replaces Arg (R)	1
NMeArg6 replaces Arg (R)	1
Aze replaces Pro (P)at position 4 , HomoArg6 replaces Arg (R)	1
Aze replaces Pro (P)at position 4 , 4GuanPhe6 replaces Arg (R)	1
Aze replaces Pro (P)at position 4, NMeArg replaces Arg (R) at position 6	1
Tryptophan (W) at position 3 is replaced with Phe, alanine (A) at position 5 is replaced with Tyr	1
HomoArg replaces Arg (R) at position 6,Tryptophan (W) at position 3 is replaced with Phe, alanine (A) at position 5 is replaced with Tyr	1
4GuanPhe replaces Arg (R) at position 6,Tryptophan (W) at position 3 is replaced with Phe, alanine (A) at position 5 is replaced with Tyr	1
NMeArg replaces Arg (R) at position 6,Tryptophan (W) at position 3 is replaced with Phe, alanine (A) at position 5 is replaced with Tyr	1
HomoArg replaces Arg (R) at position 6,Tryptophan (W) at position 3 is replaced with Phe, alanine (A) at position 5 is replaced with Tyr, Aze substituitons at position 4	1
4GuanPhe replaces Arg (R) at position 6,Tryptophan (W) at position 3 is replaced with Phe, alanine (A) at position 5 is replaced with Tyr, Aze substituitions at position 4	1
NMeArg replaces Arg (R) at position 6,Tryptophan (W) at position 3 is replaced with Phe, alanine (A) at position 5 is replaced with Tyr, Aze substituitions at position 4	1
Linker Z = Structure mentioned in patent, dSer substituitions at position 2	1
Conjugation of palmitic acid, biotinylated labelling, , (AzF) was incorporated into the position 126 on the repebody followed by lipid conjugation	1
D143A amino acid substituition	1
E32K, E34S amino acid substituition	1
Fusion of Human Relaxin 2 with Fc IgG using linker	5
O: L-ornithine at position 2	1
ADI was conjugated to dextran- reactive aldehyde groups via the formation of aldimine linkage	5
Fluorescence dye	2
K12C modification, fluorescence dye	1
K12C modification, fluorescence dye, PEG(5KDa) conjugation at Lys27	1
Fluorescence dye, PEG40 conjugation at Lys27	1
Lys27 conjugaged with (PEG(10KDa)-HGEGTFTSDLSCQMEEEAVRLFIEWLKNGGPSSGAPPPS)	1
C6 and C13 linked with S4 = Structure given in paper, residue 8 modification with Nle, residue 23 modifcation with hArg	1
Ser23 linked with X3 = Structure givven in paper	1
O=Ornithine	2
Cy3 conjugation	6
Inserting valine to the X amino acid position in the EBP (VPGXG) sequence, labeled with Flamma® 675 vinylsulfone	1
Labeled with Flamma® 675 vinylsulfone	1
C6 fatty acid linked between	2
R amino acid substituition at 1,4, 11, FAM denotes 5,6-carboxyfluorescein conjugated with Orn,p=D-Proline6,O=Ornithine8	1
R amino acid substituition at 1,4, 11, FAM denotes 5,6-carboxyfluorescein conjugated with Orn,p=D-Proline11,O=Ornithine7	1
Glycine (amino acid 2) modifcation	1
4xPEG10KDa modification at Lys26 through transient linker	2
PEG40KDa modification at Lys26 through permanent linker	1
3H labeling at Tyr, Ser8 modification	8
Lys9, d-Tyr(Et)11 modification in NT(8–13)	1
d-Tyr(Et)11 modification in NT(8–13)	1
Lys8, d-Arg9, d-Tyr(Et)11] modification in NT(7–13)	1
Fluorophore indocyanine green (ICG) at Lysine27	5
Lys1 linked with Har = Homo-Arginine, GlyΨ[Trl] is a glycyl-1,2,3-triazole unit mimicking glycine (triazole ring substitution instead of peptide bond)	1
GlyΨ[Trl] is a glycyl-1,2,3-triazole unit mimicking glycine (triazole ring substitution instead of peptide bond)	1
Diethylaminopropyl isothiocyanate (DEAP) conjugation at Lys1 side chain	1
N-methylation at Phe7	2
Lys-34 is replaced by Arg and Lys-26 is acylated with a C16 palmitic acid linkd with γGlu	9
T639I mutation	2
Asp2 and Lys3 were replaced with their D-isomers	2
R2=H	3
R2=Me, Methylation at Glu8	3
R2=Me, Methylation at Gln5	1
R2= Me, Methylation at Gln8	6
R2=Me, Methylation at Glu5	2
sTyr = Sulfated-Tyrosine, Nle = Nor-leucine, DMeAsp = N-methylated DAsp	1
Phe(4sm) = 4-sulfomethylphenylalanine, Nle = Nor-leucine, MeAsp = N-methylated Asp	1
Phe(4sm) = 4-sulfomethylphenylalanine, Nle = Nor-leucine, DMeAsp = N-methylated D-Asp, MePhe = Methylated-phenylalanine	6
sTyr = Sulfated-Tyrosine, Nle = Nor-leucine, DMeAsp = N-methylated DAsp, MePhe = Methylated-phenylalanine	1
Nle = Nor-leucine, DMeAsp = N-methylated D-Asp, MePhe = Methylated-phenylalanine	3
sTyr = Sulfated Tyrosine, Nle = Nor-leucine, DMeAsp = N-methylated D-Asp, MePhe = Methylated-phenylalanine	1
sTyr = Sulfated Tyrosine, Nle = Nor-leucine, DMeAsp = N-methylated D-Asp, MePhe = Methylated-phenylalanine, Me1Nal = N-methyl-1-naphthylalanine	2
sTyr = Sulfated Tyrosine, Nle = Nor-leucine, DMeAsp = N-methylated D-Asp, MePhe = Methylated-phenylalanine, Phe(4sm) = 4-sulfomethylphenylalanine, βAsp at position 1	1
(1Nal),(D-Ala) at position 3,(tBuGly) at Asp14	4
Lys10 linked with (OEG-Cotinine-OEG-SSSPIQGSWTWENGKWTWKGIIRLEQ-NH2), D-alanine	1
B-D1A Cys mutation	2
B-S29C,D1A Cys mutation	5
Lys15 linked with (Cot-Mal-PEG4-Ala-SN38)	1
V69M/I80T/F83L mutation in D6.1	1
K46M/K75X/N79M/ K142I mutations on D6.2	1
K30E/I41F/X75K/T135I/I142K mutation on El.1	1
K142I mutation in El.3	1
Q77E mutation	1
T136V mutation in D6.4	1
Q77E mutation in D6.5	1
X1 =G , X2= A	7
X1 =K, X2= E	4
X1 =R, X2= E	1
X1 =K, X2= D	2
X1 =R, X2= D	1
Peptides are attached via a GGGSK linker to the nanocarrier surface via a thioether-mediated conjugation	2
Sulfo-Cy5 fluorophore	8
Rhodamine labeling	6
N23G24	4
N29G30	4
N111G112	4
N184G185	4
N238G239	4
N196A197	4
N360A361	4
R=OMe	1
R=Me	1
R=F	1
R=Cl	1
N216A217	4
N278A279	8
chemical group (S)-3-amino-3-(1-naphthyl)-propionic acid- conjugated between R1 and Lys2	1
chemical group (S)-3-amino-3-(1-naphthyl)-propionic acid- conjugated between R1 and F2	1
Introduction of Cys at C terminal of Exendin-4	1
MeAla, MeArg,Lys1 modified with Myr	1
MeAla, MeArg	2
All D-amino acids	1
Conjugation of Palmitic acid at Lys20 (single monomer) , dimerization	2
Substituition of G for A at position 2	7
Acetate	4
Palmitic-Glu conjugation at Lys	4
X3 = structure given in paper	7
X4 = structure given in paper	1
X1 = structure given in paper	6
X2 = structure given in paper	6
D-Phe	1
Thio substiuition in Asp (analogue 11) and Phe (analogue 9b)	1
Methylation at Phenylalanine (D-form)	1
Cys17-Gly8-GLP-1(7-36) modification and fatty acid modification through Mal referred to as X1	1
Cys17-Gly8-GLP-1(7-36) modification and fatty acid modification through Mal referred to as X2	1
Cys17-Gly8-GLP-1(7-36) modification and fatty acid modification through Mal referred to as X3	1
Cys37-Gly8-GLP1(7-36) modification and fatty acid conjugation through Mal at Cys37 referred to as X1	1
Cys37-Gly8-GLP1(7-36) modification and fatty acid conjugation through Mal at Cys37 referred to as X2	1
Cys37-Gly8-GLP1(7-36) modification and fatty acid conjugation through Mal at Cys37 referred to as X3	1
125I-labeled, VH and VL joined by G4S linker	1
125I-labeled, 2 ScFv joined by G4S linker	1
125I-labeled, 3 ScFv joined by G4S linker	1
125I-labeled, 4 ScFv joined by G4S linker	1
K6T modification	1
Dimerization using GS linker	1
Lipidation at Lys14 (C16-yE-)	1
68Ga labelling	4
Ala2 was substituted with Gly	1
Trp3 → Phe3, Pro4 → Aze4, Ala5 → Tyr5, Arg6 → HArg6, Leu8 → Ala(ψCH2NH)6 substituitions	6
HArg, Aze substituitions	1
Interconnected through a diethylene glycol (DEG) spacer	2
X= allylglycine, Nle = Nor-leucine	11
X= allylglycine, Rx=Na-ally-arginine, Nle = Nor-leucine	2
X= allylglycine, Sx=Na-allyl-serine, Nle = Nor-leucine	1
All D-amino acids except Gly	18
Dmt = 2',6'-dimethyltyrosine at position 4	1
N(benzyl)Gly modfication at position 4	1
N(4-OH-Phenethyl)Gly at position 4	1
Oic = octahydroindole carboxylic acid modification between R5 and R6	1
1,3-bis(bromomethyl)benzene linker (L5) for stapling i, i+4 spacing	1
Phe355 -> Asp355 modification	1
A and B chain linked with disulfide bond, B3E, desB27, modifications	1
A and B chain linked with disulfide bond,A21A, B3E, desB27 modifications	2
A and B chain linked with disulfide bond,B28D,modifications	1
A and B chain linked with disulfide bond,B28D, modifcations	2
A and B chain linked with disulfide bond,A21A, B3E, desB27,modifications	1
A and B chain linked with disulfide bond,A21A, B3E, desB27, modifcations	1
A and B chain linked with disulfide bond, A21A, B3Q, desB27, modifications	1
A and B chain linked with disulfide bond, B3E, desB27, modififcations	1
A and B chain linked with disulfide bond,B3E, desB27,modificaitons	1
A and B chain linked with disulfide bond, modifications	1
A and B chain linked with disulfide bond,A21A, B3E, desB27, modificaitons	1
A and B chain linked with disulfide bond,A21A, B3Q, desB27, modifications	1
A and B chain linked with disulfide bond,modifications	1
125I labeld at His9	4
Tetramerization using PEG2000	1
ClY20/62/171 modifications, ClY = 3-Chloro-Tyrosine	1
Cy5 dye (Lumiprobe) were chemically conjugated to the amine groups of lysine residues on the exterior surface of the nanocages	1
Gly-rich linker (GSSGGSGSSGGSGGGDEADGSRGSQKAGVDE) is used, Cy5 dye (Lumiprobe) were chemically conjugated to the amine groups of lysine residues on the exterior surface of the nanocages	4
Ala5 substituition in GpTx-1	1
K573P modification in HSA,GLP-1 modified with PEG-maleimide	1
K34R substituition at GLP-1, Conjugated with indomethacin via γGlu attached to the ε-amine of Lys26 of the GLP-1 analog	1
K34R substituition at GLP-1, at Lys20 indomethacin is linked through a γGlu residue-Lys, DIF=diflunisal, Dehydroxylation of DIF	1
Aib modification at position 2, 20	7
Dimer joined by linker La - SGLEA–(EAAAK)4–ALEA–(EAAAK)4–ALEGS	1
Lys4 linked with Palm fatty acid	6
Linked by (G4S)3 linker	1
D-amino acid substituitons	2
X2 = Structure given in paper, n= 40	1
X3= Structure given in paper, n = 108	1
substituting –NHCO– amide bond of Ala2 with –CH(CF3)NH– to form (A'), Lys20 conjugation with C18, K34R modification	1
Substituiting Asn28 with Gln28	2
L-ornithine (Orn)	1
Ala2 to Gly2	1
X1=Asn at position 1, X2=Leu at position , X3=Lys,X4 = Thr, Biotinylated Lysine	1
X1=Asn, X2=Leu, X3=Lys,X4 = Thr, Biotinylated Lysine	2
X1=D-Asn, X2=Leu, X3=Lys,X4 = Thr, Biotinylated Lysine	1
X1=D-Asn, X2=Leu, X3=Lys, Biotinylated Lysine	1
y = D-Tyr	4
Substituting arginine 14 with alanine	1
O denotes L-ornithine	4
TAMRA-labeled	4
PEGylation at Cys14 through Mal-modified PEG20K, TAMRA-labeled	1
D-amino acid substituitons Trp	2
Aib, DLeu,ProNle, D-Ala	1
Aib, DLeu,DGln, ProNle, D-Arg at position 3	1
x = Val,Gly or Ala	8
Tz4 = triazole linker	2
Substituition of amino acids G,L,K,Q,M,E,E,V,R,L,E,K,N,O,P,S,S,G,A,P,P,P,S	4
Lys4 conjugated with Palm	1
y = D-Tyr, cyclic peptide linked with ZW800-1	1
(D185N, D186N, E478Q) amino acid modifications	2
Ala-modified SN38 (Cys-Mal-PEG4-Ala-SN38) linked with Cys-modified APT EDB through Lys15	1
c = D-Cys at position 1	1
Pen, Thz = Penicillamine, Thiazolidine	1
Pen, Thz = non-natural amino acid	1
c = D-Cys and Pen, Thz, Sar = non-natural amino acid	1
c = D-Cys and Sar modification , Pip = Pipecolic acid	1
c = D-Cys and Pen, Pip = non-natural amino acid	1
c = D-Cys and Sar,Pen, Pip = non-natural amino acid	1
Nle = Norleucine at position 11	1
Nle = Norleucine at position 12	1
Nle= Nor-leucine at position 11, Aib = 2-Aminoisobutyric acid at position 12	1
Gly9 was exchanged with Lys, TAMRA = 5,6-carboxytetramethylrhodamine at Lys9 modification at Lysine , Nle= Nor-leucine at position 11, Aib = 2-Aminoisobutyric acid at position 12	2
O = L-ornithine, (WO)2 repititive motifs substituited	1
O = L-ornithine, (WO)3 repititive motifs substituited	1
O = L-ornithine, (IO)2 repititive motifs substituited	1
O = L-ornithine, (IO)3 repititive motifs substituited	1
GLP-1 variant (A8G/G26E/R36G) linked to the human IgG2σ constant heavy-chain by a peptide linker (GGGSGGGSGGGS)	1
Substitution of the Pro7 to Gly and Leu8 to a Lys appended with a polyethylene glycol space and a palmitoyl group, Palm = Palmitic acid	3
K1, Dpr3 = Diaminopropionic acid,E8 substituitions and Pam = Palmitoylation modification at side chain of Lys1	1
Nα-Methylation of Lysine at position 33, K1, Dpr3 = Diaminopropionic acid,E8 substituitions and Pam = Palmitoylation modification at side chain of Lys1	2
123I labeling	1
X3(Fatty acid structure given in paper) linked with Ser11	1
D-Phe at position 4	1
Replacing Trp8 with the more bulky unnatural Dip = Diphenyalanine	2
Cys addition at C terminal of Ex4	1
R14A substituitions	1
Leu31 substituitions	5
β3-homophenylalanine (β3-hPhe) at position 3 and 6	2
β3-homophenylalanine (β3-hPhe) at position 3 and 6, substitution of Phe with Tyr at positions 4 and 7	1
Fluorescently labeled with Alexa Fluor	8
Two amphipathic helices linked by proline19	2
D-Phenyalanine substituitions for L-Phenylanine and Arg9 removal from C terminal	1
(f) D-Phenyalanine substituitions for L-Phenylanine (F) and Arg9 removal from C terminal	1
All D-amino acid substituitions	8
His-tag	6
Fusion with IgG Fc fragment	1
Fusion with ELP	2
enzymatically cyclized	1
Vitamin D3-PEG-maleimide	2
CTP	1

N-ter Modifications

Modification Name	Total Entries
Free	2964
Acetylation	276
Asn(Î²-D-GlcNHAc)	1
Acetylation [(C6H6)2-CO-]	1
Acetylation [(CH3)2-CH-CH2-(C6H6)-CH(CH3)-CO]	2
Acetylation (Napthalene acyl sulfonamide)	1
Acetylation(Naphthalene acylsulfonamide)	1
Acetylation [(C6H6)-(C6H12)-(C6H6)]	1
Acetylation (Naphthalene)	1
Acetylation [(C6H6)(CH2)4CH3]	1
PyroGlutamic acid at 1st position	5
Sar	2
(NMe)Sar	2
N.A.	37
Methoxy-polyethylene glycol-Succinimidyl Carbonate (SC-mPEG, molecular weight 20 kDa, named SC-mPEG20k )	1
Methoxy-polyethylene glycolPEG-aldehyde (mPEG-ALD10k )	1
2-indolyl-propionyl	1
2,4-dichlorophenoxyacetic acid with (CH2)n-spacers	375
Glycosylation	7
Saturated acyl chain of 4 carbons	1
Saturated acyl chain of 8 carbons	1
Saturated acyl chain of 12 carbons	1
Saturated acyl chain of 16 carbons	1
1-Î²-mercaptopropionic acid	2
Pegylated by addition of PEG5000	1
Pegylated by addition of PEG12,000	1
Addition of Polyvinyl pyrrolidone(PVP6,000)	1
Chex =Cyclohexane carboxylic acid	2
Methoxypoly(ethylene glycol)-aldehyde (mPEG-ALD)	1
Human transferrin protein	1
Pegylation	11
Human serum albumin	3
Hexanoylation	2
alpha-hydroxybutyric acid	2
Methylation	1
Beta-Alanine1	2
Beta-Glu1	2
Beta-Asp1	2
Hydroxylation of N-terminal of Glycine	2
Beta-Alanine	1
Modification of His1 of Exendin-4 into dimethylhistidyl (DM) group	1
Modification of His1 of Exendin-4 into desaminohistidyl (DA) group	2
Modification of His1 of Exendin-4 into betahydroxylamidazolpropionyl (HY)	1
Modification of His1 of Exendin-4 into imidazoacetyl (CA) group	1
Pegylation [40kdaPEG linked to INFÎ±2 via 2-sulfo-9-fluorenylmethoxycarbonyl (FMS)]	1
5-Fluoro-4-N-succinamoyl	4
N4- Boc	1
Mpr=mercaptopropionyl	2
Dextran 70kDa conjugation	1
13 amino acid extension peptide at the N-terminus of IGF-I	4
N-alpha-(alpha-D-glucosyl(1-4)-1-deoxy-D-fructosyl)	1
NHIsp	1
Succinylation	5
2-aminooctanoic acid	1
Mu (Morpholino)	2
Sar=Sarcosine	2
Sialic acid	1
Lactic acid	1
Lactose	2
Bn-glutarylation	1
Myristoylation	5
Nicotinoylation	1
Fluoryl amide	1
Chlorpheniramine M	2
Cbc=Cyclobutanecarboxylic acid	1
5(S)-benzamido-4-oxo-6-phenylhexanoyl	1
Cu-DOTA (DOTA=1,4,7,10- tetraazacyclododecane-1,4,7,10-tetraacetic acid)	2
Pegylated with 20,000 mw PEG	1
Pegylated with 20,000 mw PEG [CH30(CH2CH2O)nCH@CH2C=O]	24
5-oxo	5
PyroGlu=Pyroglutamic acid	1
177Lu,DO3A-CH2CO-G-(4-aminobenzoyl)	2
Pegylation-PEG750	1
Pegylation-PEG2000	1
5-(and-6)-carboxytetramethylrhodamine(TAMRA)	2
C12-Laa	1
Two C12-Laa	1
N-Î²-D-glucosamine succinamic acid(GlcNS)	1
DBCO modified S10 at C terminus	1
IsoV = Isovaeryl at position 1	8
P1h3	3
Conjugation of angiotensin-converting enzyme 2 (ACE2)-derived peptide A1 to the N terminus of the viral HR2-derived peptide HR2m through a long flexible linker,	5
GLP-1 molecule was linked to the N-terminus of ABD via a (GGGGS)3 linker (GLP-ABD), His-tag	2
Conjugating 18F nuclide with a modified KE108 peptide, MPAA modification at N terminal	1
N terminal amine group of His replaced by imidazo-acetyl	13
Exendin-4 peptide (Ex) fused to the N-terminus of the DARPin (DARP) protein via (GGGGS)3, His-tag and TEV protease site introduced at position 1	1
Au gold particle conjuagtion at N terminal through formation of Au-S bond	4
23 amino acid leader sequence of cystatin S introduced at N terminal	2
Fused with IgG2 Fc chain via (Gly-Ser)10 linker, Fc-fragments consisting of the CH2 and CH3 domains of the heavy chain and hinge regions of human IgG2 Fc modified as follows: The first and second cysteines of the hinge region were replaced with serine to prevent detrimental disulfide bridge formation; the last amino acid (lysine) of the Fc region was replaced with an alanine	1
QQT* conjugated with IRDye800 at C terminus using linker	1
Conjugation with human immunoglobulin G Fc-binding peptide (IBP) at n terminus	2
Polysarcosine = poly(N-methyl glycine)	3
Single nanometer iron oxide and PEG conjugation at N terminal	1
pGlu = Pyroglutamate	35
Ac modifed Lysine in Palmitic fatty acid linked with B7-33 using PEG linker	1
Ga labelling, conjugation of AAZ3A-endoHB-NCS to c(RGD)(cyclo(Arg-Gly-Asp-D-Phe-Lys) peptide at N terminus	1
Onc72 N-terminally coupled via a short peptide linker LVPR to 5 kDa thiol PEGs	4
Onc72 N-terminally coupled via a short peptide linker LVPR to 20 kDa thiol PEGs	4
Tripeptide linker {5-aminopentanoic acid [Ape(5)]–Glu–Asp} of 1 was replaced by a shorter linker (γ-D-Glu), X = Structure given in paper	1
[(1H-imidazol-4-yl)-acetyl 1]	1
Fluorescently labelled	14
Lys side chain conatins Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1	2
Lys side chain conatins Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1	1
Lys side chain conatins Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1 ,	1
Lys side chain conatins Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl attached to Lys1	1
D-Lys conjugated with [(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]	2
Chem. 16 [(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1	2
Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to L-Aeg	1
Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1	3
Chem. 17[(4S)-4-carboxy-4-(17-carboxyheptadecanoylamino)butanoyl] attached to Lys1	2
Chem. 22[(2S)-2,6-bis[[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]hexanoyl] attached to Lys1	1
Chem. 16 [(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to G-Aeg	1
Chem. 19[2-[[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]acetyl] attached to Lys1	1
Chem. 21[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to D-Lys1	1
Alb23 fused at the N-termini of both Fc domains of efgartigimod	6
ABD (albumin Binding Domain)	1
Cystatin S	1
IgG Fc linked at N terminus through MAL-PEG-ALD linker	6
N-octanoyl	5
sNEP (amino acid 52–749 of NEP) recombinantly linked to a single-chain fragment constant (scFc) of mouse IgG2c antibody at N terminus using linker	2
Aza-Phe at postion 1	6
Modified at position 1 with an aza-amino acid (aza-arginine)	1
Replacing tyrosine (Tyr) with 2,6-dimethyltyrosine (Dmt) at position 1	4
IgG1 Fc linked with hAM using linker (GGGGS)3	2
IgG4 Fc linked with hAM using linker (GGGGS)3	2
DSPE-PEG	3
desH indicates the non-natural amino acid deamino-histidine	5
desH indicates the non-natural amino acid deamino-histidine at position 1	7
Lys1 linked with (palmitoyl-Glu-OH)	4
PEG4	4
3A coupled to bicyclononyne-modified MSs (MS-N-hydroxysuccinymidocarbonates)	2
3B coupled to bicyclononyne-modified MSs (MS-N-hydroxysuccinymidocarbonates)	2
PEGylation (mPEG)	1
Single-chain variant of insulin has modifications:TyrB16Glu,PheB25His,ThrB27Gly,ProB28Gly,LysB29Gly,ThrB30Gly,IleA10Thr,TyrA14Asp,AsnA21Gly, single-chain variant of insulin with B-chain linked to A-chain by a short linker (Linker 1)	6
DTX	2
Flexible 35-mer linker (L35) connects the FN3 domain to the EK1 peptide at N terminus	1
FN3 domain	1
C18 diacid-gGlu-2xOEG	7
GFP	4
68Ga labelled	3
D-val at position 1	3
Oxazole-2-carbonyl, D-val at position 1	5
12 KDa PEG	1
Alb=albumin	1
Dextran	1
Streptavidin	1
G5-PAMAM4	1
k=D-Lysine,Sar=N-terminal glycine, N£-octadecanoyl	1
Frap (A Fusion Tag)	3
N-Acetylated Arg2	1
Lys1 acetylation	1
FC [CF3(CF2)7(CH2)2C(O)] conjugation at N terminal	1
Gly1(A) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with chondroitin [CH]	6
Gly1(A) Maleimide modified linked using linker C6 (N-[ε-maleimidocaproyloxy] sulfosuccinimide ester, EMCS) with chondroitin [CH]	4
Gly1(A) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) with chondroitin [CH]	4
Gly1(A) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with heparosan [HPN]	4
Gly1(A) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) withheparosan [HPN]	2
Hoo = L-hydroorotic acid	1
Maleimide	1
64Cu labeling	2
6-aminohexanoic acid (Ahx) linker is anchored between the N terminus of the peptide and the (DOTA) 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid , 64Cu labeling	2
pGlu = Pyroglutamate at position 1	1
Gd4	1
ABD	1
HC = Hydrocinnamate, O1: ornithine	3
Genetic fusion of modified GLP-1 to the N-terminal of DARPins through a flexible linke (GGGGS)3 further DARPin linked with another DARPin using PT-linker	1
Genetic fusion of modified GLP-1 to the N-terminal of DARPins through a flexible linke (GGGGS)3	1
Fluorocarbon chain (CF3(CF2)7(CH2)2C(O)) attached to the N-terminal part of K17F	1
Fluorocarbon chain (CF3(CF2)7(CH2)2C(O)) to the N-terminal part of K17F	1
N terminal of Tyr linked with NH bond with R1 = Structure given in paper	2
OPT substituted with an N-methyl proline at position 1	1
Radiolabelled with 111ln, DOTA, EvansBlue dye	1
Radiolabelled with 111ln, DOTA	1
FITC-Ahx	3
DNP	8
FITC labelled	5
Thiol bisphosphonate,Maleimidopropionyl,PEG conjugated at N terminus	2
GLP-1 7–36 peptide is linked to the light chain N-terminal of the TB01-2 antibody via a (G4S)x3 linker	1
DOTA	4
PEG-CDM	2
3XFLAG labelling	2
Both Arg residues in positions 1 and 2 were replaced by two Lys	1
125I labeled	1
GM-CSF O-glycosylated Peptide	1
Modified GOMP	1
mPEG5	2
C14 labeling	1
Acetylation, 177Lu Labelling	1
N-Lauryl	8
N-myristoyl	8
Acetylation, N-terminus of apelin-13 linked via, liphophilic moiety pIPhe polypeptide spacer (-γGlu-OEG-OEG-) with C6	2
Acetylation, N-terminus of apelin-13 linked via, liphophilic moiety pIPhe polypeptide spacer (-γGlu-OEG-OEG-) with C13	2
Acetylation, N-terminus of apelin-13 linked via, liphophilic moiety pIPhe polypeptide spacer (-γGlu-OEG-OEG-) with C15	2
Acetylation, N-terminus of apelin-13 linked via, liphophilic moiety pIPhe polypeptide spacer (-γGlu-OEG-OEG-) with C17	2
Acetylation, N-terminus of apelin-13 linked via, liphophilic moiety pIPhe polypeptide spacer (-γGlu-OEG-OEG-) with C6 diacid	2
Acetylation, N-terminus of apelin-13 linked via, liphophilic moiety pIPhe polypeptide spacer (-γGlu-OEG-OEG-) with C18-diacid	2
Fc joined with ELA-21 by linker (GGGS)3	1
KK amino acid substiuitions	7
Kψ[CH2NH]K substiuition at position 1	1
Kψ[CH2NH]K substiuition	8
Aminoisobutyric acid	3
68Ga-DOTA-(p-aminomethylaniline)-(diglycolic acid), D-Phe at position 1	2
mPEG2000, 89Zr labeling	1
GLP-1 A8G modification linked by GSGG	1
Linker	1
Linker (GGAAG)	1
Linker (GAGAAG)	1
Carboxyl-terminal peptide (CTP) of the human chorionic gonadotropin β su bunit and N-linked glycosylation sequences were linked to rhIFN-α2b at N terminus	1
Fluorescein	2
Radiolabelled with 64Cu	1
Leucine reduction	1
X = Struture given in paper (6b)	3
HA = Hyaluronic acid hydrogel linked with GLP-1 analogue	1
2A-Gossypol Conjugate Linked By Thiazolidine Imine Linkage	1
Bodipy Tr-X Ester Linked Via (Peg)12	1
IBP conjugation to the N-terminus of CP24	1
Repebody	3
Gu: N,N,N',N' tetramethylguanidino	9
Acetylation	6
L-Arg replaced with D-Arg at position 1	1
EX acylation with LA (Lactic acid)	1
hIgG4 Fc conjugation through linker AEAAAKEAAAKEAAAKEAAAKA	1
2 kDa PEG conjugated to the N-terminus of cC34 through Mal linker	1
5 kDa PEG conjugated to the N-terminus of cC34 through Mal linker	1
DOX	2
FAM denotes 5,6-carboxyfluorescein	1
Proline substituition (amino acid 1)	1
PEG5KDa through permanent linker	2
Conjugation of amino groups of the lipids of liposomes with CAR peptide at N terminal Cys	4
AOPC8 = 1‑(2‑(2‑aminophenyl)‑2‑oxoethyl)‑1H‑pyrrole‑2‑ carboxylic acid (AOPC)	2
AOPC8 = 1‑(2‑(2‑aminophenyl)‑2‑oxoethyl)‑1H‑pyrrole‑2‑ carboxylic acid (AOPC), d-Arg9 modification at N terminal	1
D-Lys at the first position which contains Har = Homo-Arginine side chain	1
Lys at the first position contains Har = Homo-Arginine side chain	1
Dap (2,3-diaminopropionic acid) substiuition at 1st position	1
Side chain of the Lys residue in the first position was extended by attaching additional homoarginine (Har)	1
Dab (2,4-diaminobutyric acid) substiuition at 1st position	1
CS (chondroitin sulfate)	1
KLA linked with PsTag216 using flexible linker GGGGS at N terminal	1
R1 = NH2-Lys-Phe-Arg	6
R1 = PALM-Lys-Phe-Arg	6
R1 = PEG-Lys-Phe-Arg	6
Chitooligosaccharide chloride	1
yGlu-(OEG)2 linker between C18 fatty acid and peptide	6
yGlu-(OEG)2 linker between C18 fatty acid and peptide	3
yGlu-(OEG)2 linker between C14 fatty acid and peptide	1
yGlu-(OEG)2 linker between C16 fatty acid and peptide	1
yGlu-(OEG)2 linker between C20 fatty acid and peptide	1
yGlu-PEG10-PEG10 linker between C18 fatty acid and peptide	2
C18 fatty acid	1
Lys(C18d-yGlu-(OEG)2) linker between hydroxyphenylacetic acid and peptide	1
FITC-GSHP	1
A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488	15
10K PEG	2
20K PEG	2
40K PEG	2
SATHA-FBA	5
Fluorescein isothiocynate labeled	2
PCL-PEG	2
C18-EEG	1
Stearic acid conjugation	1
6FAM labelled	3
ES2	1
ES2-AF peptide was conjugated with HA by the formation of an amide linkage between the amino group of the ES2-AF peptide and the activated carboxyl of HA	1
CH90 linked by linker EDA–(LMDS)	2
CH30/CH40/CH70 linker by linker	1
PEG30K	2
PEG10K	1
125I labelled	7
64Cu-DOTA	2
Fc linked by (GGGS)3 linker at N terminus	1
CH2CO chemical group attached, DOTA conjugated with Lys1	4
Replaced the Nterminal Ala with an acetyl group	5
99mTc-HHEDEG	2
Maleimide joined by linker PEG24	2
Palm-Maleimide joined by linker PEG24	2
C16-Maleimide joined by linker PEG24	2
C18-Maleimide joined by linker PEG24	2
Chol-Maleimide joined by linker PEG24	4
Chol-PEG5K-Maleimide joined by linker PEG24	2
Chol-Maleimide joined by linker PEG31	4
Amidation	1
MPB-Mal modified, additional cysteine residue on N-terminus of SP	4
Acetylation, 7-OH-Tic = 7-hydroxy-L-1,2,3,4- tetrahydroisoquinoline-3-carboxylic acid at position 1	1
Ac-2'NaI = 2’-naphtylalanine at position 1	1
DD	1
FAM	4
68Ga-NOTA	1
99MTC-HHEDEG-DEG	1
FITC conjugation	1
Ghrelin (12-28)	2
Reversed sequence ghrelin(28-12) fused to the N-terminal side of CNP(6-22)	1
Met addition at N terminal of G-CSF	2
tag	5
Fluorescein (F)	3
Tag-3xPEG24	2
PEGylation (20KDa)	1
PEGylation (40KDa)	1
Fluoresceinisothiocyanate labelled	1
Dox = Doxorubicin, Cys incorporation for linking	1
Tetra PEG hydrogel linked with exenatide using linker MeSO2-	2
Tetra PEG hydrogel linked with exenatide using linker -CN	2
Gu: N,N,N′,N′-tetramethylguanidine, O denotes L-ornithine	3
AAYR	1
LVPR	1
111In-DTPA = diethylenetriaminepentaacetic acid	4
111In-DTPA-Gly = diethylenetriaminepentaacetic acid	1
CTP fused to hGH	27
PEG5K	1
PEG20K	1
D-amino acid Phe	2
CF3(CF2)7(CH2)2C(O)	1
Conjugation of KTP cyclic peptide at N terminal	4
X1 = biotin-PEG3 label	2
99Mtc Radiolabeled	3
N-Terminally fused to a leader signal sequence from the NS1 protein	1
Pr = propionylation, c = D-Cys at N terminal	5
Palmitic acid conjugation	3
mPEG(2KDa)-Maleimide	1
Tam (6-Carboxytetramethylrhodamine) labeling, Glycine substitution at position 1	5
HSA joined using a linker	1
Conjugation of HA into CTX at N terminal in IONP-HA-GEM	1
Fatty acid moiety attached to Ser1 at N terminal	1
R8( structure given in paper) at NH terminal	1
R2( structure given in paper) at NH terminal	1
R5( structure given in paper) at NH terminal	1
R7( structure given in paper) at NH terminal	1
R9( structure given in paper) at NH terminal	1
CTP ( the terminal peptide of the β subunit of human chorionic gonadotropin (hCG))	2
7 mer ABD domain conjugated at N terminus	1
conjugating a truncated antimicrobial peptide B28 to the N-terminus of the tumor-homing peptide bombesin	1
3H labeling at N terminal	2
SarLys = N-methyl glycine and Lysine	2
3H labelled	8
P1 Substituitions From Kersmf	2
P1 From KERsmf	1
His7 of GLP1	2
Stapled	3
acetylate	1
6-his tag, free cysteine	1
removing Œ±-carbon of histidine	1
20K-PEG	1
VitD-(25)-PEG2K	1
VitD-(3)-PEG1.2K	1
VIP with a Met	1
Fc	2
lipid	1
hFC	1
VIP	1
SAH	3

C-ter Modifications

Modification Name	Total Entries
Free	2215
Amidation	1024
Pegylation	8
N.A.	37
XTEN	2
NH-3,5-Bzl(CF3)2	4
Biotinylation with PEG spacer	375
Human serum albumin	3
NHBn	24
Y= structure given in paper	36
CH2CH2Ph	15
Cholesterol moiety	2
O-[3 €™,5 €™-(CF3 )2 Bzl]	1
NH-[3 €™,5 €™-(CF3 )2 Bzl]	5
Propylamidation	10
Hexylamidation	3
Dimerization using PEGylation	4
Ethylamide	17
XTEN-288	1
Fusion of Alpha-1 Antitrypsin Monovariant [Î±1AT(P357N)]	1
Addition of maleimidopropionic acid (MPA) and amidation	4
Addition of hydroxyl group	2
Addition of Fc	8
Linking IgG1 using CEx-Linker (SSGAPPPS-GGGGSGGGGSGGGGS)	2
Addition of NH2-PEG at Cys40	3
Benzyl ester-2(1H)-pyrimidone	2
2-(1H)-pyrimidone	2
5-FC (5 Fluorocytosine)	1
Isobutyl citrate	27
PMO (5'-ACGTTGAIIIGCATCGTCGC-3')	6
Tc chelator (NC100194)	2
lys coupled to the chelator DOTA (DOTA is 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid)	1
Addition of lycinamide	2
N-Ethylmaleimidation	15
Beta-alanine-PEG	10
D-glucopyranuronamide	2
Cyclopamine	2
Fc region	4
Amidated CPA	3
Methy esterification	1
OL	1
Ethylacetate	5
Thiolated carboxymethyl dextran(CMD) cysteine conjugated via disulfide bond	1
Pegylation (PEG750)	1
Pegylation (PEG2000)	1
Ahx-6-aminohexanoic acid, Mpa-3-maleimidopropionic acid conjugated to the amino group of Ahx,XTEN protein	1
DBCO modified S11 peptide at N terminus	1
Fc region of IgG joined through (CH2-CH3) IgD	3
His-tag	3
Cys modified PTH-1 linked with VitD3 through (PEG)36	8
Sul = Sulpiride	1
Linked with Chol using PEG2k linker	1
Replacing the amide bond with a C-terminal acid	4
Chol conjugation at C terminal	4
ABD was connected to the N-terminus of the XTEN polypeptide (144 amino acids) through a (GGGGS)3 linker	1
ABD was connected to the N-terminus of the XTEN polypeptide (288 amino acids) through a (GGGGS)3 linker	1
The amino group of KE108 peptide conjugated with the carboxyl group of NODA	1
FGF21 fused to the C-terminus of the DARPin (DARP) protein via (GGGGS)3 linker	1
Fusion of CD	1
PEG4 spacer was designed and subsequently reacted with a cysteine at the carboxyl terminus then, the elongated thiol-modified homodimer peptide was conjugated with DOX	1
Relaxin-A chain linked with albVHH domain at C terminus, A and B chain linked by linker	4
Amidation, Orn=Ornithine at position 19	5
Amidation, Orn at position 23	8
PEGylation (Rh(4.4 ± 1.1nm)) and linked via DBCO	2
PEGylation (Mw(46.3KDa)) and linked via DBCO	1
POEGMA (poly[oligo(ethylene glycol) methyl ether methacrylate]) conjugation (MW opt = 54.7KDa)	3
Conjugation of GT15912 and hIgG4 Fc was carried out through the formation of amine bonds between the bi functional PEG and Lys34 in GT15912 or the N-terminal amino acid in hIgG4 Fc	1
Exendin-DBCO was conjugated to azide-functional PEG(27.7KDa)	2
Exendin-DBCO was conjugated to azide-functional PEG(46.3 KDa)	1
Exendin-DBCO was conjugated to azide-functional POEGMA(54.7KDa)	2
Alb23 fused at the C-termini of both Fc domains of ABDEG via a 20GS linker	6
ABD (albumin Binding Domain)	2
PEG Rh(27.7Kda)	2
PEG MW(46.3 Kda)	1
PEGMAopt(54.7Kda)	1
POEGMAopt(54.7Kda)	1
POEGMA conjugation	1
Terminal Lys side chain linked to C16 fatty acid via linker yE-C16 at C terminal	1
HMC001	6
NHEt (Ethylamine)	4
Leuprolide acetate with the hydroxyl groups of leuprolide acetate	1
ScFc then attached to the BBB transporter (scFv8D3) at C terminus using linker	2
Amidation, Aza-glutamic acid (azaE4) modification at position 4 (E4)	1
Aza-glutamic acid (azaE4) modification at position 4 (E4)	1
Amidation, Q amino acid subtituition at place of E at C terminal	2
Amidation, Aza-glutamine (azaQ4)	2
Six lysines has been added at C terminal	1
Two lysines has been added at C terminal	3
1 lysines has been added at C terminal	3
Six lysines has been added at C terminal , Amidation	2
Conjugation to MMAE cytotoxin via a valine–citrulline (V-Citr) cleavable linker,Val-Citriline linker and BTC joined by spacer Sar10	11
MTP/RGD comodified with CAL/TAN NS	1
MTP/RGD comodified with CAL/TAN NS (PEG-DSPE)	1
Glu3 linked with (PEG4-c(RGDfK))2	4
Glu linked with [PEG4-c(RGDfK)]2	4
Interdomain linker (Linker 2) connecting the A-chain of insulin to the Fc and the Fc domain from IgG2	6
ZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linker	18
A short linker GKG was attached at C terminal and then ALbumin tag was linked with Lys via PEG2	4
Amidation, GGPSSGAPPPS introduced in the C-terminal	6
PNAM37 linked through NH2 group	1
Selenium methylated conjugation at C terminal	1
Amidation, FLAG tag	10
Ec (E.coli) SsrA tag sequences conjugation	1
Mf (M.fluorum) SsrA tag sequences	2
Ec (E.coli) SsrA tag sequences	1
Albumin binding Nanofitins (ABNF) linked at C terminus by 4 aa	2
Albumin binding Nanofitins (ABNF) linked at C terminus by 7 aa	2
Albumin binding Nanofitins (ABNF) linked at C terminus by 12 aa	1
Albumin binding Nanofitins (ABNF) linked at C terminus by 25 aa	1
βAlanine at C terminal conjugation	1
GFP	7
Amidation, 3-Pal modification at C terminal	6
Cy5 linked with Lys side chain at C terminus	4
Cy5 linked with Lys side chain at C terminus, PEGylation	1
Fab heavy chain linked to C terminus of ScFv light chain	5
B29R, desB30 modifications	9
B29R, desB30 modificaiton	1
B29R, desB30 modification	11
Tyr13 modifcation, carboxylation	3
Val13 modifcation, carboxylation	2
Ala13 modifcation, carboxylation	2
K29(B) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with chondroitin [CH]	4
K29(B) Maleimide modified linked using linker C6 (N-[ε-maleimidocaproyloxy] sulfosuccinimide ester, EMCS) with chondroitin [CH]	4
K29(B) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) with chondroitin [CH]	4
K29(B) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with heparosan [HPN]	2
K29(B) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) with heparosan [HPN]	2
Ethylene Diamine-modified chondroitin90 (CH) linked with C terminus of GLP-1C using linker C12 , (N-[λ-maleimidododecanoyloxy]-sulfosuccinimide ester (sulfo-LMDS, C12 derived from LMDS)	2
Ethylene Diamine-modified heparosan (HPN) linked with C terminus of GLP-1C using linker C12 , (N-[λ-maleimidododecanoyloxy]-sulfosuccinimide ester (sulfo-LMDS, C12 derived from LMDS)	2
Methyl amide addition at C terminus	1
Methylated Tyr36 at C terminus	1
Methylated Arg35 at C terminus	1
Methylated Gln34 at C terminus	1
Methylated Arg33 at C terminus	1
β-homoTyr36 at C terminus	1
β-homoArg35 at C terminus	2
β-homoGln34 at C terminus	1
β-homoArg33 at C terminus	1
MeArg35 at C terminus	1
DOX	1
HSA linked through PEG4	1
TP5 conjugation	1
Cys addition at C terminal	1
15aa linker, enzyme cleavable site, PAS(40), 5 aa flexible linker conjugated at C terminus	1
Add RGDK tretapeptide to HFn-PAS C-terminus	1
Add RGDK tretapeptide to HFn-PAS C-terminus and substituite enzyme cleavable linker with PLGLAG	1
Ex4 linked to DNP9 = Dinitro phenol by (PEG)n spacer	1
Ex4 linked to DNP10 = Dinitro phenol by (PEG)n spacer	1
Ex4 linked to DNP11 = Dinitro phenol by (PEG)n spacer	1
PEG20 KDa, MeO	8
HSA	4
Cisplatin (CDDP) is complexed with the carboxyl groups of the L-glutamic acid	5
Lys146 contains Fatty acid moiety which introduces 8-amino-3,6-dioxaoctanoic acid (AEEA) and glutamic acid	4
substitution of Leu13 by the (L)-(Trimethylsilyl)-Alanine (TMSAla)	1
scFv of 8D3 is added to SST	1
Aminoethylamide -NH-CH(CH2-CH(CH3)2)2	1
IgG1 Fc	3
PAS#1(600)	2
TRAIL joined with ATNC using flexible linkers consisting of small amino acids (GSGGGSG) that could form a bridge between the C-terminal of TRAIL and the triple helix	1
TRAIL joined with ATNC using flexible linkers consisting of small amino acids (GSGGGSG) that could form a bridge between the C-terminal of TRAIL and the triple helix followed by (MMP2) cleavage site (GPLGLAG) then IL4rP (CRKRLDRNC)	1
Either or nonsulfated gastrin-6 were coupled to the C-terminus of 2d and 2k through two OEG spacers, affording 5a−5d	2
4c, 4d, 4m, and 4n were next C-terminally modified with the sequence Tyr-Gly-Trp-Leu-Asp-Phe-NH2 using two OEGs as the linker to generate 6a−6d	4
fusion of the C-terminus of NRG1 to the N-terminus of the Fc fragment	1
C-terminus of 1F7 is directly fused to the Fc fragment	1
C-terminus of ALM6 is directly fused to 1F7	1
AFF	1
ABD	1
ABD-AFF	2
Tyrosine (Y) residue was added to E5 sequence and 125I was added	1
Gemicitabine	5
TMSAla conjugation	4
TMSAla-OH conjugation	4
Folate peptide (FA-Pep-1) conjugated to EGCG-loaded nanoparticles (EGCG-NPs)	1
bisMal-PEG(10KDa)	3
NH-CH[CH2-CH(CH3)2]2 chemical group attached at C terminal	2
Cy5.5 labelling	1
Addition of the 12 C-terminal residues of Ex-4 to a C-terminal truncated OXM, amidation	1
Carboxyl-terminal peptide (CTP) of the human chorionic gonadotropin β subunit and N-linked glycosylation sequences were linked to rhIFN-α2b at C terminus	1
Carboxyl-terminal peptide (CTP) of the human chorionic gonadotropin β su bunit and N-linked glycosylation sequences were linked to rhIFN-α2b at C terminus	1
hIgG4 Fc-linker-AP25	6
KKKKKK amino acids substiuitions at C terminal	1
E5B9	1
One 4-carboxy-3-fluorophenylboronic acid (PBA), Three cholic acids (CA)	2
PEG-P(CL-DTC)	1
IgG4 hinge-Fc fragment	1
Proline addition at C terminal	1
GLP-1(7-36) (A8G) fused to the off-target repebody through linker (A(EAAAAK)3A) at C terminus	1
GLP-1(7-36) (A8G) fused to the repebody in complex with HSA through linker (A(EAAAAK)3A) at C terminus	2
Cys40 conjugation at C terminal, PEG(40 KDa)	1
TP5 conjugated with LTP(13-36) at C terminus	1
Human C-peptide genetically conjugated at the C-terminus of nine repeats of lysine-containing elastin-like polypeptide	6
Ten repeats of EBP without a linker sequence, (EBP)10 fused at the C-terminus of the exenatide for Ex-(EBP)10, 6xHis tag	1
lm7-FH fusion	1
lm7-FH-SA21	1
lm7-PEG30K	1
lm7-PEG2*20K	1
PA-600-6H	4
PA-600	6
Dab (2,4-diaminobutyric acid)	1
VEGFR1-selective hexapeptide (GNQWFI, AF) ,amidation	2
Conjugation between Ex-Mal-DBCO and N3−Lys-Fc	3
Conjugated with Cy5.5	2
(DAC) maleimidopropionic acid conjugated with Equine serum albumin	1
Bis-maleimide-NH2	1
Bis-maleimide-C16 conjugation at C terminal	1
palmitic acid (C16) was conjugated to the C-terminus of YIK (at Lys37) with a linker GSG between C16 and YIK	1
PAS#1(200)	1
Dox conjugation	1
Replaces the seventh residue (proline) with a serine, and has a glucose sugar moiety attached to the serine and is amidated on the C terminus	3
FITC	2
FA-01	1
FA-02	2
FA-08	1
FA-09	1
SPG C2 domain	2
D-Α-Tocopherol Succinate Linked Via Peg	2
C-Terminal End Of The Ar Peptide Was Added With An Nh2-Rich Linker (GGGGKKKK)	1
Au	1
Human chorionic gonadotropin β subunit carboxyl-terminal peptide (CTP) and an N-glycosylation sequence linked to its C-terminus	1
Human chorionic gonadotropin β subunit carboxyl-terminal peptide (CTP) and an N-glycosylation sequence linked to its C-terminus via linker	1
Substituition of Phe with Lys at C terminal	1
PEG(20k)	4
Additional C terminal cysteine linked to peptide using dislufide bond	1
C terminal Cys extension for bis-maleimide linkage	2
HPN50 linked by linker EDA–(LMDS)	2
CH10 linked by linker	1
Met substituition at C terminal	12
maleimidopropionic acid (MPA) at the C-terminal	1
PLGA linked through mPEG	1
Chlorambucil	4
Melphalan	4
Bendamustine	4
CCPEG	4
Cterminal extension following the C-terminal alanine composed of 3 sarcosines and 2 D-arginine residues	6
Acetylation	1
ABD domain from Streptococcal G strain , Amidation	2
mCherry	1
Fc	3
C-type lectin domain of human SP-D joined with Strep-tag II using linker	2
B29K(N(Eps)Tetradecanedioyl-4×gGlu), desB30 modifications	5
B29K(N(Eps)Tetradecanedioyl-gGlu-2xOEG), desB30 modifications	3
B29K(N(Eps)Tetradecanedioyl-gGlu-2×OEG), desB30 modifications	2
B29K(N(Eps)Tetradecanedioyl-4×gGlu), desB30 modifications	1
B29K(N(Eps)Tetradecanedioyl), desB30 modifications	1
B29K(N(Eps)Hexadecanedioyl-gGlu-2×OEG), desB30 modifications	1
B29K(N(Eps)Hexadecanedioyl-4×gGlu), desB30 modifications	1
B29K(N(Eps)Hexadecanedioyl-gGlu), desB30 modifications	1
ELK16 short peptide was introduced to the C-terminus of ThXylC	1
HCG	1
Deamidation at C terminal	6
Ghrelin (12-28)	3
Ghrelin(12-28)amide	1
Ghrelin(12-28)	1
Fusing the XTEN peptide of 36 amino acids through a linker	1
Fusing the XTEN peptide of 72 amino acids through a linker	1
Fusing the XTEN peptide of 144 amino acids through a linker	1
Fusing the XTEN peptide of 288 amino acids through a linker	1
GLP-1 modified PEG-Mal group reacts with the free C34 of rHSA, chemical group attached between Lys31 (8-amino-3,6-dioxaoctanoyl-maleimidopropionyl) and D32	2
Diflunisal is linked to the GLP-1 peptide through its hydroxyl group	1
Acylated at a C-terminal lysine with a saturated C16 lipid	7
ABD035	1
X4 = D-Thr at C terminal	1
C-terminal part of exenatide was connected to the N-terminal part of APTHSA using a long (18-mer) linker	1
ZW800-1 fluorophore	2
Chitosan-modified SeNP (SC)	1
2 CTP fused	27
eTGFBR2 fused at the C-terminal of HSA	1
(ATS) was fused to the C-terminus of the anti-RV scFv57R	2
RCCMs	1
PEG-PLC	1
PEG-P(TMC-DTC)	1
sHDL	4
Pro(4-Br)Phe substituition	2
lfreW = D and L -amino acids	1
eeird = D-amino acids	1
ABP-G148 (Albumin binding protein) conjugation	2
Zw800-1	1
Rt1.14	1
poly(2-methacryloyloxyethyl phosphorylcholine)	2
Human IgG2σ constant heavy-chain linked via a peptide linker (GGGSGGGSGGGS) with human GLP-1 (A8G/G26E/R36G) at C terminal	1
PEG-Stp = succinoyl-tetraethylene pentamine/NIS gene	1
HSA joined using a linker	1
TPGS(D-a-tocopherol polyethylene glycol succinate) linked with poly(lactide) using disulfide linkage, cRGD further conjugated to NP surface	1
PEG(2KDa) linked with Ex-4 through Mal (Maleimide)	1
PEG(5KDa) linked with Ex-4 through Mal (Maleimide)	1
PEG(20KDa) linked with Ex-4 through Mal (Maleimide)	1
(PEG(50KDa))3 linked with Ex-4 through Mal (Maleimide)	1
tEB (Truncated Evans blue) dye linked via Maleimide	1
Cy5.5 labeled	1
CTP ( the terminal peptide of the β subunit of human chorionic gonadotropin (hCG))	2
AEBMP: N-(2-(2-(2-(2-aminoacetamido)acet-amido)acetamido) ethyl)-2-bromo-2-methylpropanamide, OEGMA(54.6KDa)	1
AEBMP: N-(2-(2-(2-(2-aminoacetamido)acet-amido)acetamido) ethyl)-2-bromo-2-methylpropanamide, OEGMA(55.6KDa)	1
AEBMP: N-(2-(2-(2-(2-aminoacetamido)acet-amido)acetamido) ethyl)-2-bromo-2-methylpropanamide, OEGMA(71.6KDa)	1
TFacetate = Trifluoroacetate addition at C terminal	1
Acetate addition at C terminal	1
IgG4 Fc fused at C terminal using GS linker	2
Poly[Oligo(Ethylene Glycol)9 Methyl Ether Methacrylate] = Poegma(54.6 Kda)	1
Poly[Oligo(Ethylene Glycol)3 Methyl Ether Methacrylate] = Poegma(55.6Kda)	1
Poly[Oligo(Ethylene Glycol)3 Methyl Ether Methacrylate] = Poegma(71.6Kda)	1
T1 From KERsmf	1
T1 Substituitions From Kersmf	1
T2 Removed	2
Stapled	1
amidated	1
182P	1
cysteine	1
3CTPs	1
thiol group	1
Fusion with ELP	4
ELP(1-120)	1
hFC	1
ELP (1-120)	1
SAH	2

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