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• W2000758416 abstract "Peptides with alternating hydrophobic and polar amino acids have been shown to form stable beta-sheet secondary structures and self-assemble into hydrogel-like matrices in the presence of physiological salt concentrations. We hypothesized that the sequence and steric size differences of non-polar residues can affect the balance of peptide intermolecular forces in solution that drive self-assembly. To test this hypothesis, we designed a library of artificial amphiphilic peptides based on the sequence (FEFEFKFK)2 by substituting combinations of the non-polar residues glycine, alanine, valine, leucine and isoleucine for phenylalanine. Peptide structure and self-assembly were characterized using scanning electron microscopy, the Thioflavin T assay, transmission electron microscopy, X-ray fiber diffraction and circular dichroism spectroscopy. The sequence and steric size of non-polar residues are shown to cause variations in peptide secondary structures and create significant differences in the matrix morphology of self-assembled peptides." @default.
• W2000758416 created "2016-06-24" @default.
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• W2000758416 date "2005-09-01" @default.
• W2000758416 modified "2023-10-18" @default.
• W2000758416 title "Effects of the sequence and size of non-polar residues on self-assembly of amphiphilic peptides" @default.
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• W2000758416 doi "https://doi.org/10.1016/j.ijbiomac.2005.06.006" @default.
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