Details of SAPdb entry with Sequence YL |
| Primary information | |
|---|---|
| SAPdb ID | 1358, |
| PMID | 24256076 |
| Peptide Name | YL |
| Peptide sequence | YL |
| N-Terminal Modification | Fmoc(fluorenylmethoxycarbonyl) |
| C-Terminal Modification | Free |
| Non-Terminal Modification | None |
| Length | 2 |
| Peptide/Conjuagate | Peptide |
| Technique | AFM (Atomic Force Microscopy, Fluorescence Emission Spectroscopy and DLS (Dynamic Light Scattering) |
| Solvent | 100mM Phosphate buffer |
| Method | self-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 %. |
| Conc | 10mM |
| Temperature | pH 8 |
| Temperature | Room temperature |
| Incubation Time | 2 hours |
| Year | 2013 |
| Self assembly | Yes |
| Type of Self assembly | Hydogel (consists of Nanofibers) |
| Tertiary Structure (Technique) | Not Predicted), |
| Linear | |
| NA | |
| NA | |
| Hydrogel | |
| 100 | |
| YL | |
| N.A. | |
| Primary information | |
| SAPdb ID | 1361, |
| PMID | 24256076 |
| Peptide Name | YL |
| Peptide sequence | YL |
| N-Terminal Modification | Fmoc(fluorenylmethoxycarbonyl) |
| C-Terminal Modification | Free |
| Non-Terminal Modification | None |
| Length | 2 |
| Peptide/Conjuagate | Peptide |
| Technique | AFM (Atomic Force Microscopy, Fluorescence Emission Spectroscopy and DLS (Dynamic Light Scattering) |
| Solvent | 100mM Phosphate buffer |
| Method | self-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 %. |
| Conc | 10mM |
| Temperature | pH 8 |
| Temperature | Room temperature |
| Incubation Time | 3 - 6 hours |
| Year | 2013 |
| Self assembly | Yes |
| Type of Self assembly | Hydogel (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, |
| PMID | 24256076 |
| Peptide Name | YL |
| Peptide sequence | YL |
| N-Terminal Modification | Fmoc(fluorenylmethoxycarbonyl) |
| C-Terminal Modification | Free |
| Non-Terminal Modification | None |
| Length | 2 |
| Peptide/Conjuagate | Peptide |
| Technique | AFM (Atomic Force Microscopy, Fluorescence Emission Spectroscopy and DLS (Dynamic Light Scattering) |
| Solvent | 100mM Phosphate buffer |
| Method | self-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 %. |
| Conc | 10mM |
| Temperature | pH 8 |
| Temperature | Room temperature |
| Incubation Time | 3 - 6 hours |
| Year | 2013 |
| Self assembly | Yes |
| Type of Self assembly | Hydogel (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, |
| PMID | 21107375 |
| Peptide Name | Dipeptide 3 |
| Peptide sequence | YL |
| N-Terminal Modification | Fmoc(fluorenylmethoxycarbonyl) |
| C-Terminal Modification | Free |
| Non-Terminal Modification | None |
| Length | 2 |
| Peptide/Conjuagate | Peptide |
| Conjugate partner | None |
| Technique | AFM (Atomic Force Microscopy) and DLS (Dynamic Light Scattering) |
| Solvent | Sodium phosphate buffer (pH 8) |
| Method | Peptide 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. |
| Conc | 10 mmol/kg |
| Temperature | 8 |
| Temperature | Intial 55°C heating for 1 hour and followed by cooling at room temperature |
| Incubation Time | 72 hour |
| Year | 2010 |
| Self assembly | Yes |
| Type of Self assembly | Transparent gel |
| Tertiary Structure (Technique) | Not Predicted), |
| Linear | |
| NA | |
| Stable | |
| Hydrogel | |
| NA | |
| YL | |
| N.A. | |
| Primary information | |
| SAPdb ID | 1618, |
| PMID | 24896538 |
| Peptide Name | Fmoc-YL |
| Peptide sequence | YL |
| N-Terminal Modification | Fmoc(fluorenylmethoxycarbonyl) |
| C-Terminal Modification | Free |
| Non-Terminal Modification | None |
| Length | 2 |
| Peptide/Conjuagate | Peptide |
| Conjugate partner | None |
| Technique | SEM (Scanning Electron Microscopy) and AFM (Atomic force Microscopy) |
| Solvent | Phosphate buffer |
| Method | 0.5mM 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. |
| Conc | 10mM |
| Temperature | 8 |
| Temperature | Room temperature |
| Incubation Time | 24 hours |
| Year | 2014 |
| Self assembly | Yes |
| Type of Self assembly | Gel (consist of Fibrous network) |
| Tertiary Structure (Technique) | Not Predicted), |
| Linear | |
| NA | |
| NA | |
| Hydrogel | |
| NA | |
| YL | |
| N.A. | |
| Primary information | |
| SAPdb ID | 1619, |
| PMID | 24896538 |
| Peptide Name | Fmoc-YL |
| Peptide sequence | YL |
| N-Terminal Modification | Fmoc(fluorenylmethoxycarbonyl) |
| C-Terminal Modification | Free |
| Non-Terminal Modification | None |
| Length | 2 |
| Peptide/Conjuagate | Peptide |
| Conjugate partner | None |
| Technique | SEM (Scanning Electron Microscopy) and AFM (Atomic force Microscopy) |
| Solvent | Chlorofom |
| Method | 25mM 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. |
| Conc | 10mM |
| Temperature | 8 |
| Temperature | Room temperature |
| Incubation Time | 24 hours |
| Year | 2014 |
| Self assembly | Yes |
| Type of Self assembly | Gel (consist of Fibrous network) |
| Tertiary Structure (Technique) | Not Predicted), |
| Linear | |
| NA | |
| NA | |
| Hydrogel | |
| NA | |
| YL | |
| N.A. | |
| Primary information | |
| SAPdb ID | 1620, |
| PMID | 24896538 |
| Peptide Name | Fmoc-YL |
| Peptide sequence | YL |
| N-Terminal Modification | Fmoc(fluorenylmethoxycarbonyl) |
| C-Terminal Modification | Free |
| Non-Terminal Modification | None |
| Length | 2 |
| Peptide/Conjuagate | Peptide |
| Conjugate partner | None |
| Technique | SEM (Scanning Electron Microscopy) and AFM (Atomic force Microscopy) |
| Solvent | Phosphate buffer |
| Method | 10 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. |
| Conc | 10mM |
| Temperature | 8 |
| Temperature | Room temperature |
| Incubation Time | 24 hours |
| Year | 2014 |
| Self assembly | Yes |
| Type of Self assembly | Gel (consist of Fibrous network) |
| Tertiary Structure (Technique) | Not Predicted), |
| Linear | |
| NA | |
| NA | |
| Hydrogel | |
| NA | |
| YL | |
| N.A. | |