Details of SAPdb ID 1013 |
Primary information | ||
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SAPdb_ID | 1013 | |
PMID | 12714741 | |
Year | 2003 | |
Name | NH2-L-Phe-L-Phe-COOH | |
Sequence | FF | |
N-Terminal Modification | Free | |
C-Terminal Modification | Free | |
Non-terminal Modication | None | |
Length | 2 | |
Peptide/Conjugate/Mixture | Peptide | |
Conjugate Partner | None | |
Technique | Transmission Electron Microscopy (TEM) | |
Solvent | Aqueous dispersion | |
Method | NH2-L-Phe-L-Phe-COOH dipeptide solublized at very high concentrations ( >=100 mg/ml) by dissolving the lyophilized peptide in 1,1,1,3,3,3 hexafluoro-2-propanol. The peptide appeared to be highly soluble in the organic solvent, a rapid assembly into ordered semicrystalline structures was observed visually within seconds after dilution into the aqueous solution at a final µM concentration range. | |
Concentration | >=100 mg/ml stock soln | |
pH | NA | |
Temperature | 80 °C | |
Incubation Period | Within few minutes | |
Self-Assembly Formation | Yes | |
Type of Self-Assembly | Nanotube | |
Size of Self-Assembled structure | Nanotube diameter varied from 50-250nm | |
Linear/Cyclic | Linear | |
Stability of Nanostructure | After 1 hour of incubation of the Phe-Phe peptide with proteinase K (0.02 mg/ml), no tubular structures were observed by electron microscopy examination (as compared with hundreds of tubular structures observed before the proteolysis). | |
Comment | NA | |
Secondary information | ||
Physico-Chemical properties |
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STRUCTURE |
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SMILES | N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc1ccccc1)C=O |