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Amphipathic peptides have an increased propensity to self-assemble into amyloid-like β-sheet fibrils when their primary sequence pattern consists of alternating hydrophobic and hydrophilic amino acids. These fibrils adopt a bilayer architecture composed of two β-sheets laminated to bury the hydrophobic side chains of the β-sheet in the bilayer interior, leaving the hydrophilic side chains exposed at the bilayer surface. In this study, the effects of altering the sequence pattern of amphipathic peptides from strictly alternating hydrophobic/hydrophilic repeats to more complex patterning of hydrophobic and hydrophilic residues on self-assembly of the resulting sequences is reported. Self-assembly of the Ac-(FKFE)₂-NH₂ peptide was compared to that of four related sequences with varied amino acid sequence patterning: Ac-(FK)₂(FE)₂-NH₂, Ac-KEFFFFKE-NH₂, Ac-(KFFE)₂-NH₂, and Ac-FFKEKEFF-NH₂. The Ac-(FKFE …