Balancing hydrophobicity and sequence pattern to influence self‐assembly of amphipathic peptides
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DOI: 10.1002/bip.23099
Abstract: Amphipathic peptides with alternating polar and nonpolar amino acid sequences efficiently self‐assemble into functional β‐sheet fibrils as long as the nonpolar residues have sufficient hydrophobicity. For example, the Ac‐(FKFE)2‐NH2 peptide rapidly self‐assembles into β‐sheet bilayer… read more here.
Keywords: self assembly; hydrophobicity; phe; amphipathic peptides ... See more keywords