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Details of SAPdb entry with Sequence LG
Primary information
SAPdb ID 1282,
PMID20307067
Peptide NameFmoc-Leu-Gly-OH
Peptide sequenceLG
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueTransmission Electron Microscopy (TEM), Scanning Electron Microscopy (SEM)
SolventNaCl solution containing hydroquinone
MethodA stock solution of 0.24 mol dm-3 of dipeptide derivative in DMSO was prepared. Then 10 μL of the stock was added to 1 cm-3 of a solution containing 0.066 mol dm-3 hydroquinone and 0.1 mol dm-1 NaCl. Then 4 μL of 1 mol dm-3 NaOH was added to fully dissolve the dipeptide and 8 μL of 1 mol dm-3 HCl to bring pH 7. The final solution was introduced to the surface of the gold slide via an electrochemical flow cell.
Conc1mg/ml
Temperature< 4
Incubation Time2 hours
Year2010
Self assemblyYes
Type of Self assemblyHydogel Membranes
Tertiary Structure
(Technique)		Not Predicted),
Linear
NA
Stable under acidic conditions on applying current
Hydrogel
NA
LG
N.A.
Primary information
SAPdb ID 1286,
PMID22890605
Peptide NameFmocLG
Peptide sequenceLG
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagateConjugate
Conjugate partnerFmoc(fluorenylmethoxycarbonyl)
TechniqueScanning Electron Microscopy (SEM)
SolventSodium hydoxide(0.1 M )
MethodA 0.5 wt% stock solution of dipeptide at pH 9 – 10 prepaed by adding 1 equivalent of sodium hydroxide solution 0.1 M solution) with stirring to dissolve, 0.1 M HCl added to lower the pH of solution o 5. To form gels, 2 mL of stock solution was placed in a 7 mL Sterilin cup and UV light was irradiated from a 40 W Spectroline X-series UV lamp (wavelength 254 nm) .
Conc5mg/ml
Temperature5
TemperatureRoom temperature
Incubation Time14 hours
Year2012
Self assemblyYes
Type of Self assemblyOpaque gel (Nanofibers)
Tertiary Structure
(Technique)		Not Predicted),
Linear
NA
NA
Hydrogel
70
LG
N.A.
Primary information
SAPdb ID 1444,
PMID24085660
Peptide NameFmoc-LG
Peptide sequenceLG
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueTransmission Electron Microscopy (TEM) and WAXS(Wide Angle X - Ray scattering)
SolventWater + 0.1M Hcl + 0.5 M NaOH
MethodFmoc-dipeptide was suspended in water. Sodium hydroxide (0.5 M) was gradually added to the aqueous suspensions of Fmoc-dipeptide until pH 10.5 was reached. The samples were vortexed and sonicated for one minute to fully dissolve the peptide amphiphiles. To obtain required pH, a required volume of dilute hydrochloric acid (0.085 M) was then added dropwise to the solution. Solution sonicated and vortexed. Next, the samples were heated to 75–80 ◦C until fully dissolved and homogenised. The samples were subsequently cooled and maintained at 4 ◦C for ∼ 12 hours (overnight) to promote gelation.
Conc10mmol/L
Temperature10.5
Temperature4 °C
Incubation Time~ 12 hours
Year2013
Self assemblyNo
Type of Self assemblyNo hydogel formation
Tertiary Structure
(Technique)		Not Predicted),
Linear
NA
NA
None
NA
LG
N.A.
Primary information
SAPdb ID 1445,
PMID24085660
Peptide NameFmoc-LG
Peptide sequenceLG
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueTransmission Electron Microscopy (TEM) and WAXS(Wide Angle X - Ray scattering)
SolventWater + 0.1M Hcl + 0.5 M NaOH
MethodFmoc-dipeptide was suspended in water. Sodium hydroxide (0.5 M) was gradually added to the aqueous suspensions of Fmoc-dipeptide until pH 10.5 was reached. The samples were vortexed and sonicated for one minute to fully dissolve the peptide amphiphiles. To obtain required pH, a required volume of dilute hydrochloric acid (0.085 M) was then added dropwise to the solution. Solution sonicated and vortexed. Next, the samples were heated to 75–80 ◦C until fully dissolved and homogenised. The samples were subsequently cooled and maintained at 4 ◦C for ∼ 12 hours (overnight) to promote gelation.
Conc10mmol/L
Temperature7.6
Temperature4 °C
Incubation Time~ 12 hours
Year2013
Self assemblyYes
Type of Self assemblyNanoribbon
Tertiary Structure
(Technique)		Not Predicted),
Linear
NA
NA
Nanoribbon
24
LG
N.A.
Primary information
SAPdb ID 1446,
PMID24085660
Peptide NameFmoc-LG
Peptide sequenceLG
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueTransmission Electron Microscopy (TEM) and WAXS(Wide Angle X - Ray scattering)
SolventWater + 0.1M Hcl + 0.5 M NaOH
MethodFmoc-dipeptide was suspended in water. Sodium hydroxide (0.5 M) was gradually added to the aqueous suspensions of Fmoc-dipeptide until pH 10.5 was reached. The samples were vortexed and sonicated for one minute to fully dissolve the peptide amphiphiles. To obtain required pH, a required volume of dilute hydrochloric acid (0.085 M) was then added dropwise to the solution. Solution sonicated and vortexed. Next, the samples were heated to 75–80 ◦C until fully dissolved and homogenised. The samples were subsequently cooled and maintained at 4 ◦C for ∼ 12 hours (overnight) to promote gelation.
Conc10mmol/L
Temperature 4.3 - 5.6
Temperature4 °C
Incubation Time~ 12 hours
Year2013
Self assemblyYes
Type of Self assemblyTwisted Ribbon
Tertiary Structure
(Technique)		Not Predicted),
Linear
NA
NA
Nanoribbon
13.5
LG
N.A.
Primary information
SAPdb ID 1477,
PMID22651803
Peptide NameDipeptide4
Peptide sequenceLG
N-Terminal ModificationNapthalene
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueScanning Electron Microscopy (SEM) and X - Ray Diffraction
SolventWater + 0.1 M NaOH
Method25mg of dipeptide was suspended in deionized 5ml water . An equimolar amount of NaOH (0.1 M,aq) was added, and the solution was gently stirred until a clear solution was formed. Glucono-Å’Â¥- lactone (GdL) was added to the solution and the samples were gently swirled to dissolve the GdL before being left to stand for 24 h without stirring to form gel.
Conc5mg/ml or 0.5%wt
TemperatureRoom temperature
Incubation Time24 hours
Year2012
Self assemblyYes
Type of Self assemblyTransparent or clear gel
Tertiary Structure
(Technique)		Not Predicted),
Linear
NA
NA
Hydrogel
NA
LG
N.A.
Primary information
SAPdb ID 1483,
PMID22651803
Peptide NameDipeptide13
Peptide sequenceLG
N-Terminal ModificationNapthalene
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueScanning Electron Microscopy (SEM) and X - Ray Diffraction
SolventWater + 0.1 M NaOH
Method25mg of dipeptide was suspended in deionized 5ml water . An equimolar amount of NaOH (0.1 M,aq) was added, and the solution was gently stirred until a clear solution was formed. Glucono-Å’Â¥- lactone (GdL) was added to the solution and the samples were gently swirled to dissolve the GdL before being left to stand for 24 h without stirring to form gel.
Conc5mg/ml or 0.5%wt
TemperatureRoom temperature
Incubation Time24 hours
Year2012
Self assemblyYes
Type of Self assemblyTransparent or clear gel
Tertiary Structure
(Technique)		Not Predicted),
Linear
NA
NA
Hydrogel
NA
LG
N.A.
Primary information
SAPdb ID 1507,
PMID20307067
Peptide NameFmoc-Leu-Gly-OH
Peptide sequenceLG
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueTransmission Electron Microscopy (TEM), Scanning Electron Microscopy (SEM) and SPR (Surface plasmon Resonance) spectroscopy
SolventDMSO + hydroquinone + NaOH + HCl
MethodStock solution of 0.24 mol/L of peptide in DMSO prepared and 10 μl of this added to 1ml of 0.066 mol dm-3 of hydroquinone and 0.1 mol dm-1 NaCl + 8 μL of 1 mol dm-3 HCl to bring pH 7. The final solution was introduced to the surface of GOLD slide via an electrochemical cell.
Conc1mg/ml
Temperature7
Year2010
Self assemblyYes
Type of Self assemblyThick layer of Hydrogel
Tertiary Structure
(Technique)		Not Predicted),
Linear
NA
Stable
Hydrogel
1000000
LG
N.A.
Primary information
SAPdb ID 1557,
PMID21833387
Peptide NamePeptide 2
Peptide sequenceLG
N-Terminal ModificationFree
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueFE - SEM (Field Emission Scanning Electron Microscopy), Transmission Electron Microscopy (TEM) and AFM (Atomic Force Microscopy)
SolventWater
MethodEach of these peptides (0.06 mmol) was dissolved in 1mLwater of pH 6.96 and allowed to age for 24 h
Conc0.06mmol
Temperature6.96
Temperature37 °C
Incubation Time24 - 48 hours
Year2011
Self assemblyYes
Type of Self assemblySpherical structure
Tertiary Structure
(Technique)		Not Predicted),
Linear
NA
Stable over wide range of pH 2 - 12
Nanosphere
95
LG
N[C@@H](CC(C)C)C(=O)NCC=O
Primary information
SAPdb ID 1713,
PMID30307451
Peptide NameFmoc-LG
Peptide sequenceLG
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/Conjuagatepeptide
Conjugate partnerNone
TechniqueUV-vis spectroscopy and BAM
Solventbulk water solution
Temperature7
TemperatureRoom temperature
Year2018
Self assemblyYes
Type of Self assemblynanostructures
Tertiary Structure
(Technique)		Not Predicted),
Linear
NA
NA
Nanostructure
NA
LG
N[C@@]([H])(CC(C)C)C(=O)NCC(=O)O
Primary information
SAPdb ID 1756,
PMID30950622
Peptide NameFmoc-LG
Peptide sequenceLG
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/Conjuagatepeptide
Conjugate partnerNone
TechniqueUV−Vis Reflection Spectroscopy and Brewster Angle Microscopy
Solventmethanol
Conc1mM
Temperature2
Temperature21 °C
Year2019
Self assemblyYes
Type of Self assemblynanomaterials
Tertiary Structure
(Technique)		Not Predicted),
Linear
NA
NA
Nanostructure
NA
LG
N[C@@]([H])(CC(C)C)C(=O)NCC(=O)O