| Autor: |
LIU, YANFEI, ZHAO, XIAOJUN |
| Předmět: |
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| Zdroj: |
NANO; Feb2011, Vol. 6 Issue 1, p47-57, 11p |
| Abstrakt: |
Branched self-assembling peptides bearing epitopes with free N-termini were designed. A lysine residue was used as branch point to present more than one epitopes in a single peptide. Atomic force microscope, circular dichroism and Fourier transform infrared spectroscopy data indicate that the N-terminus attached epitope sequences do not prevent the formation of the β-sheets and the self-assembling of these peptides into stable nanofibers in aqueous solutions. Rheology experiments show that these peptides could form self-supporting scaffolds once electrostatic repulsions were screened by electrolytes. Fluorescence spectra measurements upon binding of FITC-avidin to surfaces of nanofibers were performed to investigate the effect of charged aspartic acid residues in RGD epitopes at the lysine branching on packing and accessibility of the epitopes. Results show that the electrostatic interaction between hydrophilic side chains at branching and nanofiber surfaces may significantly affect the conformational freedom and accessibility of the epitopes at the periphery of the nanofibers. Cell entrapment experiments reveal that the attached RGD epitopes with free N-termini are biological active. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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