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Amphipathic peptides composed of alternating hydrophobic and hydrophilic amino acids are a privileged class of peptide, which have a high propensity to self‐assemble into β‐sheet fibrils. The Ac‐(FKFE)₂‐NH₂ peptide has been extensively studied and forms putative β‐sheet bilayer fibrils in which the hydrophobic Phe side chains are organized to a single face of each constituent sheet; upon bilayer formation, these hydrophobic benzyl groups are sequestered in the hydrophobic core of the resulting fibril. In order for the Phe side chains to be uniformly displayed on one face of Ac‐(FKFE)₂‐NH₂ β‐sheets, an antiparallel packing orientation in which one amino acid residue is unpaired must be adopted. Based on molecular models, we hypothesized that truncated seven amino acid derivatives of Ac‐(FKFE)₂‐NH₂ in which either the N‐terminal Phe residue (Ac‐KFEFKFE‐NH₂) or the C‐terminal Glu residue (Ac …