Details of SAPdb entry with Sequence fFV |
Primary information | |
---|---|
SAPdb ID | 1075, |
PMID | 22159641 |
Peptide Name | D-FFV. |
Peptide sequence | fFV |
N-Terminal Modification | Free |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 3 |
Peptide/Conjuagate | Peptide |
Conjugate partner | None |
Technique | Cryo - Transmission Electron Microscopy (TEM), AFM (Atomic Force Microscopy), CD (Circular Dichroism spectroscopy) and FTIR (Fourier Transform Infrared) Spectroscopy (Fourier Transform Infrared) Spectroscopy |
Solvent | 0.1M Phosphate buffer |
Method | Peptide wast dissolved in a 0.1 M sodium phosphate solution at pH 12, while subsequent dilution to final physiological pH at 7.4 triigered the formation of hydrogel at room temperature within 24 hours. |
Temperature | 7.4 |
Temperature | Room temperature |
Incubation Time | 24 hours |
Year | 2012 |
Self assembly | Yes |
Type of Self assembly | Thicker filaments and Hydrogel |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
Hydrogel | |
NA | |
None | |
N[C@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C(C)C)C=O | |
Primary information | |
SAPdb ID | 1077, |
PMID | 22159641 |
Peptide Name | FFV |
Peptide sequence | FFV |
N-Terminal Modification | Free |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 3 |
Peptide/Conjuagate | Peptide |
Conjugate partner | None |
Technique | Cryo - Transmission Electron Microscopy (TEM), AFM (Atomic Force Microscopy), CD (Circular Dichroism spectroscopy) and FTIR (Fourier Transform Infrared) Spectroscopy (Fourier Transform Infrared) Spectroscopy |
Solvent | 0.1M Phosphate buffer |
Method | Peptide wast dissolved in a 0.1 M sodium phosphate solution at pH 12, while subsequent dilution to final physiological pH at 7.4 triigered the formation of hydrogel at room temperature within 24 hours. |
Temperature | 7.4 |
Year | 2012 |
Self assembly | No |
Type of Self assembly | No self assembled structure |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
None | |
NA | |
None | |
N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C(C)C)C=O | |
Primary information | |
SAPdb ID | 1145, |
PMID | 24700146 |
Peptide Name | D-Phe-Phe-Val (II), |
Peptide sequence | fFV |
N-Terminal Modification | Free |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 3 |
Peptide/Conjuagate | Peptide |
Conjugate partner | None |
Technique | AFM (Atomic Force Microscopy), Cryo - Transmission Electron Microscopy (TEM), FTIR (Fourier Transform Infrared), CD (Circular Dichroism spectroscopy) |
Solvent | Sodium phosphate buffer |
Method | 4.2 mg of peptide were added to 300 ml of 0.1 M sodium phosphate buffer pH 11.8 and dissolved with the aid of sonication for 5 min in a water bath at room temperature, then diluted 1 : 1 with another 300 ml of 0.1 M sodium phosphate buffer pH 5.6–5.7 to yield final pH of 7.4. |
Conc | 7mg/ml |
Temperature | 7.4 |
Temperature | Room temperature |
Year | 2014 |
Self assembly | Yes |
Type of Self assembly | Twisted or elongated fibril structure |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
Nanofiber | |
NA | |
None | |
N[C@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C(C)C)C=O | |
Primary information | |
SAPdb ID | 1146, |
PMID | 24700146 |
Peptide Name | D-Phe-Phe-Val (II), |
Peptide sequence | fFV |
N-Terminal Modification | Free |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 3 |
Peptide/Conjuagate | Peptide |
Conjugate partner | None |
Technique | AFM (Atomic Force Microscopy), Cryo - Transmission Electron Microscopy (TEM), FTIR (Fourier Transform Infrared), CD (Circular Dichroism spectroscopy) |
Solvent | Sodium phosphate buffer |
Method | 4.2 mg of peptide were added to 300 ml of 0.1 M sodium phosphate buffer pH 11.8 and dissolved with the aid of sonication for 5 min in a water bath at room temperature, then diluted 1 : 1 with another 300 ml of 0.1 M sodium phosphate buffer pH 5.6–5.7 to yield final pH of 7.4. |
Conc | 7mg/ml |
Temperature | 7.4 |
Temperature | Room temperature |
Incubation Time | within Few minutes |
Year | 2014 |
Self assembly | Yes |
Type of Self assembly | Hydrogel |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
Hydrogel | |
NA | |
None | |
N[C@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C(C)C)C=O | |
Primary information | |
SAPdb ID | 1147, |
PMID | 24700146 |
Peptide Name | Phe-D-Phe-Val (III), |
Peptide sequence | FfV |
N-Terminal Modification | Free |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 3 |
Peptide/Conjuagate | Peptide |
Conjugate partner | None |
Technique | AFM (Atomic Force Microscopy), Cryo - Transmission Electron Microscopy (TEM), FTIR (Fourier Transform Infrared), CD (Circular Dichroism spectroscopy) |
Solvent | Sodium phosphate buffer |
Method | 4.2 mg of peptide were added to 300 ml of 0.1 M sodium phosphate buffer pH 11.8 and dissolved with the aid of sonication for 5 min in a water bath at room temperature, then diluted 1 : 1 with another 300 ml of 0.1 M sodium phosphate buffer pH 5.6–5.7 to yield final pH of 7.4. |
Conc | 7mg/ml |
Temperature | 7.4 |
Temperature | Room temperature |
Year | 2014 |
Self assembly | Yes |
Type of Self assembly | Filaments with globular structure |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
Other | |
NA | |
None | |
N[C@@H](Cc1ccccc1)C(=O)N[C@H](Cc1ccccc1)C(=O)N[C@@H](C(C)C)C=O | |
Primary information | |
SAPdb ID | 1148, |
PMID | 24700146 |
Peptide Name | Phe-Phe-D-Val (IV) |
Peptide sequence | FFv |
N-Terminal Modification | Free |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 3 |
Peptide/Conjuagate | Peptide |
Conjugate partner | None |
Technique | AFM (Atomic Force Microscopy), Cryo - Transmission Electron Microscopy (TEM), FTIR (Fourier Transform Infrared), CD (Circular Dichroism spectroscopy) |
Solvent | Sodium phosphate buffer |
Method | 4.2 mg of peptide were added to 300 ml of 0.1 M sodium phosphate buffer pH 11.8 and dissolved with the aid of sonication for 5 min in a water bath at room temperature, then diluted 1 : 1 with another 300 ml of 0.1 M sodium phosphate buffer pH 5.6–5.7 to yield final pH of 7.4. |
Conc | 7mg/ml |
Temperature | 7.4 |
Temperature | Room temperature |
Year | 2014 |
Self assembly | Yes |
Type of Self assembly | Globular structure |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
Other | |
NA | |
None | |
N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@H](C(C)C)C=O | |
Primary information | |
SAPdb ID | 1149, |
PMID | 24700146 |
Peptide Name | Phe-D-Phe-D-Val (II) |
Peptide sequence | Ffv |
N-Terminal Modification | Free |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 3 |
Peptide/Conjuagate | Peptide |
Conjugate partner | None |
Technique | AFM (Atomic Force Microscopy), Cryo - Transmission Electron Microscopy (TEM), FTIR (Fourier Transform Infrared), CD (Circular Dichroism spectroscopy) |
Solvent | Sodium phosphate buffer |
Method | 4.2 mg of peptide were added to 300 ml of 0.1 M sodium phosphate buffer pH 11.8 and dissolved with the aid of sonication for 5 min in a water bath at room temperature, then diluted 1 : 1 with another 300 ml of 0.1 M sodium phosphate buffer pH 5.6–5.7 to yield final pH of 7.4. |
Conc | 7mg/ml |
Temperature | 7.4 |
Temperature | Room temperature |
Year | 2014 |
Self assembly | Yes |
Type of Self assembly | Elongated fibres |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
Nanofiber | |
NA | |
None | |
N[C@@H](Cc1ccccc1)C(=O)N[C@H](Cc1ccccc1)C(=O)N[C@H](C(C)C)C=O | |
Primary information | |
SAPdb ID | 1150, |
PMID | 24700146 |
Peptide Name | D-Phe-Phe-D-Val (III) |
Peptide sequence | fFv |
N-Terminal Modification | Free |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 3 |
Peptide/Conjuagate | Peptide |
Conjugate partner | None |
Technique | AFM (Atomic Force Microscopy), Cryo - Transmission Electron Microscopy (TEM), FTIR (Fourier Transform Infrared), CD (Circular Dichroism spectroscopy) |
Solvent | Sodium phosphate buffer |
Method | 4.2 mg of peptide were added to 300 ml of 0.1 M sodium phosphate buffer pH 11.8 and dissolved with the aid of sonication for 5 min in a water bath at room temperature, then diluted 1 : 1 with another 300 ml of 0.1 M sodium phosphate buffer pH 5.6–5.7 to yield final pH of 7.4. |
Conc | 7mg/ml |
Temperature | 7.4 |
Temperature | Room temperature |
Year | 2014 |
Self assembly | Yes |
Type of Self assembly | Twisted fibril structure |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
Nanofiber | |
NA | |
None | |
N[C@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@H](C(C)C)C=O | |
Primary information | |
SAPdb ID | 1151, |
PMID | 24700146 |
Peptide Name | D-Phe-D-Phe-Val (IV) |
Peptide sequence | ffV |
N-Terminal Modification | Free |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 3 |
Peptide/Conjuagate | Peptide |
Conjugate partner | None |
Technique | AFM (Atomic Force Microscopy), Cryo - Transmission Electron Microscopy (TEM), FTIR (Fourier Transform Infrared), CD (Circular Dichroism spectroscopy) |
Solvent | Sodium phosphate buffer |
Method | 4.2 mg of peptide were added to 300 ml of 0.1 M sodium phosphate buffer pH 11.8 and dissolved with the aid of sonication for 5 min in a water bath at room temperature, then diluted 1 : 1 with another 300 ml of 0.1 M sodium phosphate buffer pH 5.6–5.7 to yield final pH of 7.4. |
Conc | 7mg/ml |
Temperature | 7.4 |
Temperature | Room temperature |
Year | 2014 |
Self assembly | Yes |
Type of Self assembly | Crystal needles |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
Nanorod | |
NA | |
None | |
N[C@H](Cc1ccccc1)C(=O)N[C@H](Cc1ccccc1)C(=O)N[C@@H](C(C)C)C=O | |
Primary information | |
SAPdb ID | 1152, |
PMID | 24700146 |
Peptide Name | Phe-Phe-Val (I) |
Peptide sequence | FFV |
N-Terminal Modification | Free |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 3 |
Peptide/Conjuagate | Peptide |
Conjugate partner | None |
Technique | AFM (Atomic Force Microscopy), Cryo - Transmission Electron Microscopy (TEM), FTIR (Fourier Transform Infrared), CD (Circular Dichroism spectroscopy) |
Solvent | Sodium phosphate buffer |
Method | 4.2 mg of peptide were added to 300 ml of 0.1 M sodium phosphate buffer pH 11.8 and dissolved with the aid of sonication for 5 min in a water bath at room temperature, then diluted 1 : 1 with another 300 ml of 0.1 M sodium phosphate buffer pH 5.6–5.7 to yield final pH of 7.4. |
Conc | 7mg/ml |
Temperature | 7.4 |
Temperature | Room temperature |
Year | 2014 |
Self assembly | No |
Type of Self assembly | Disordered structure |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
None | |
NA | |
None | |
N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C(C)C)C=O | |
Primary information | |
SAPdb ID | 1153, |
PMID | 24700146 |
Peptide Name | D-Phe-D-Phe-D-Val (I) |
Peptide sequence | ffv |
N-Terminal Modification | Free |
C-Terminal Modification | Free |
Non-Terminal Modification | None |
Length | 3 |
Peptide/Conjuagate | Peptide |
Conjugate partner | None |
Technique | AFM (Atomic Force Microscopy), Cryo - Transmission Electron Microscopy (TEM), FTIR (Fourier Transform Infrared), CD (Circular Dichroism spectroscopy) |
Solvent | Sodium phosphate buffer |
Method | 4.2 mg of peptide were added to 300 ml of 0.1 M sodium phosphate buffer pH 11.8 and dissolved with the aid of sonication for 5 min in a water bath at room temperature, then diluted 1 : 1 with another 300 ml of 0.1 M sodium phosphate buffer pH 5.6–5.7 to yield final pH of 7.4. |
Conc | 7mg/ml |
Temperature | 7.4 |
Temperature | Room temperature |
Year | 2014 |
Self assembly | No |
Type of Self assembly | Disordered structure |
Tertiary Structure (Technique) | Not Predicted), |
Linear | |
NA | |
NA | |
None | |
NA | |
None | |
N[C@H](Cc1ccccc1)C(=O)N[C@H](Cc1ccccc1)C(=O)N[C@H](C(C)C)C=O | |