Capacity for increased surface area in the hydrophobic core of β-sheet peptide bilayer nanoribbons.

ABSTRACT: Amphipathic peptides with amino acids arranged in alternating patterns of hydrophobic and hydrophilic residues efficiently self-assemble into β-sheet bilayer nanoribbons. Hydrophobic side chain functionality is effectively buried in the interior of the putative bilayer of these nanoribbons. This study investigates consequences on self-assembly of increasing the surface area of aromatic side chain groups that reside in the hydrophobic core of nanoribbons derived from Ac-(XKXE)₂ -NH₂ peptides (X = hydrophobic residue). A series of Ac-(XKXE)₂ -NH₂ peptides incorporating aromatic amino acids of increasing molecular volume and steric profile (X = phenylalanine [Phe], homophenylalanine [Hph], tryptophan [Trp], 1-naphthylalanine [1-Nal], 2-naphthylalani

SUBMITTER: Jones CW 

PROVIDER: S-EPMC8349901 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature