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Details of SAPdb entry with Sequence YL
Primary information
SAPdb ID 1358,
PMID24256076
Peptide NameYL
Peptide sequenceYL
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueAFM (Atomic Force Microscopy, Fluorescence Emission Spectroscopy and DLS (Dynamic Light Scattering)
Solvent100mM Phosphate buffer
Methodself-assembly of peptides is induced by sonicating and vortexing the Fmoc-dipeptides (10 mM) in 100 mM sodium phosphate buffer (pH 8) solution with (or without) the addition of various concentrations of proteins β- lactoglobulin (β-LG) and Bovine serum albumin (BSA) in the range of 0.03 to 0.2 wt %.
Conc10mM
Temperature8
TemperatureRoom temperature
Incubation Time2 hours
Year2013
Self assemblyYes
Type of Self assemblyHydogel (consists of Nanofibers)
Tertiary Structure
(Technique)
Not Predicted),
Linear
NA
NA
Hydrogel
100
YL
N.A.
Primary information
SAPdb ID 1361,
PMID24256076
Peptide NameYL
Peptide sequenceYL
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueAFM (Atomic Force Microscopy, Fluorescence Emission Spectroscopy and DLS (Dynamic Light Scattering)
Solvent100mM Phosphate buffer
Methodself-assembly of peptides is induced by sonicating and vortexing the Fmoc-dipeptides (10 mM) in 100 mM sodium phosphate buffer (pH 8) solution with (or without) the addition of various concentrations of proteins β- lactoglobulin (β-LG) and Bovine serum albumin (BSA) in the range of 0.03 to 0.2 wt %.
Conc10mM
Temperature8
TemperatureRoom temperature
Incubation Time3 - 6 hours
Year2013
Self assemblyYes
Type of Self assemblyHydogel (consists of Nanofibers)
Tertiary Structure
(Technique)
Not Predicted),
Linear
in presence of 0.2 % β-LG
NA
Hydrogel
110
YL
N.A.
Primary information
SAPdb ID 1364,
PMID24256076
Peptide NameYL
Peptide sequenceYL
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueAFM (Atomic Force Microscopy, Fluorescence Emission Spectroscopy and DLS (Dynamic Light Scattering)
Solvent100mM Phosphate buffer
Methodself-assembly of peptides is induced by sonicating and vortexing the Fmoc-dipeptides (10 mM) in 100 mM sodium phosphate buffer (pH 8) solution with (or without) the addition of various concentrations of proteins β- lactoglobulin (β-LG) and Bovine serum albumin (BSA) in the range of 0.03 to 0.2 wt %.
Conc10mM
Temperature8
TemperatureRoom temperature
Incubation Time3 - 6 hours
Year2013
Self assemblyYes
Type of Self assemblyHydogel (consists of Nanofibers)
Tertiary Structure
(Technique)
Not Predicted),
Linear
in presence of 0.2 % BSA
NA
Hydrogel
80
YL
N.A.
Primary information
SAPdb ID 1541,
PMID21107375
Peptide NameDipeptide 3
Peptide sequenceYL
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueAFM (Atomic Force Microscopy) and DLS (Dynamic Light Scattering)
SolventSodium phosphate buffer (pH 8)
MethodPeptide was dissolved in a 1 ml volume of 100 mM sodium phosphate buffer (pH 8) in the presence of varying concentrations of subtilisin (1.25–60.0 ml). The mixture was vortexed (30 s) and sonicated on ice for 20 min , and the low temperature ensures that no enzymatic conversion occurs up to this point. This was followed by heating,ceither in an oil bath or within the spectrophotometer using a temperature-controlled cuvet, at 55° for 60 min to allow enzymatic conversion to occur. The self-assembling system was then allowed to cool to room temperature. The gel samples were then left to stand for periods of 72 h.
Conc10 mmol/kg
Temperature8
TemperatureIntial 55 °C heating for 1 hour and followed by cooling at room temperature
Incubation Time72 hour
Year2010
Self assemblyYes
Type of Self assemblyTransparent gel
Tertiary Structure
(Technique)
Not Predicted),
Linear
NA
Stable
Hydrogel
NA
YL
N.A.
Primary information
SAPdb ID 1618,
PMID24896538
Peptide NameFmoc-YL
Peptide sequenceYL
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueScanning Electron Microscopy (SEM) and AFM (Atomic force Microscopy)
SolventPhosphate buffer
Method0.5mM Fmoc-YL solution was prepared by dissolving Fmoc-YL in 1 mL of phosphate buffer solution. After hand-shaking for 5 s emulsions form in vials. Gel formed in 24 hours on incubation at room temperature.
Conc10mM
Temperature8
TemperatureRoom temperature
Incubation Time24 hours
Year2014
Self assemblyYes
Type of Self assemblyGel (consist of Fibrous network)
Tertiary Structure
(Technique)
Not Predicted),
Linear
NA
NA
Hydrogel
NA
YL
N.A.
Primary information
SAPdb ID 1619,
PMID24896538
Peptide NameFmoc-YL
Peptide sequenceYL
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueScanning Electron Microscopy (SEM) and AFM (Atomic force Microscopy)
SolventChlorofom
Method25mM Fmoc-YL solution was prepared by dissolving Fmoc-YL in 1 mL of chloroform solution. After hand-shaking for 5 s emulsions form in vials. Gel formed in 24 hours on incubation at room temperature.
Conc10mM
Temperature8
TemperatureRoom temperature
Incubation Time24 hours
Year2014
Self assemblyYes
Type of Self assemblyGel (consist of Fibrous network)
Tertiary Structure
(Technique)
Not Predicted),
Linear
NA
NA
Hydrogel
NA
YL
N.A.
Primary information
SAPdb ID 1620,
PMID24896538
Peptide NameFmoc-YL
Peptide sequenceYL
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueScanning Electron Microscopy (SEM) and AFM (Atomic force Microscopy)
SolventPhosphate buffer
Method10 mM Fmoc-YL solution was prepared by dissolving 5.32 mg of Fmoc-YL in 1 mL of phosphate buffer solution. Different volumes of chloroform were added to Fmoc-YL buffer solution at 80 °C after hand-shaking for 5 s emulsions form in vials. Gel formed in 24 hours on incubation at room temperature.
Conc10mM
Temperature8
TemperatureRoom temperature
Incubation Time24 hours
Year2014
Self assemblyYes
Type of Self assemblyGel (consist of Fibrous network)
Tertiary Structure
(Technique)
Not Predicted),
Linear
NA
NA
Hydrogel
NA
YL
N.A.
Primary information
SAPdb ID 1798,
PMID30892363
Peptide Nameoligopeptide
Peptide sequenceYL
N-Terminal ModificationFree
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/Conjuagatepeptide
Conjugate partnerNone
Solventsodium pHospHate buffer
Conc10mM
Temperature7
TemperatureRoom temperature
Year2019
Self assemblyYes
Type of Self assemblysupramolecular complexes
Tertiary Structure
(Technique)
Not Predicted),
Linear
NA
NA
supramolecular complexes
NA
YL
N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CC(C)C)C(=O)O
Primary information
SAPdb ID 1962,
PMID28703237
Peptide NameFmoc-tyrosine-leucine (FmocYL)
Peptide sequenceYL
N-Terminal ModificationFmoc [or N-(fluorenyl-9-methoxycarbonyl)]
C-Terminal ModificationFree
Non-Terminal ModificationNone
Length2
Peptide/ConjuagatePeptide
Conjugate partnerNone
TechniqueFTIR
Year2017
Self assemblyYes
Type of Self assemblyNanofibres
Tertiary Structure
(Technique)
Not Predicted),
Linear
NA
NA
Nanofiber
NA
YL
N[C@@]([H])(Cc1ccc(O)cc1)C(=O)N[C@@]([H])(CC(C)C)C(=O)O