Methyl‐Blocked Dimeric α,γ‐Peptide Nanotube Segments: Formation of a Peptide Heterodimer through Backbone–Backbone Interactions

Abstract

Cyclic peptides can dimerize through β-sheet-like hydrogen bonding. Heterodimerization is favored over homodimerization, which creates interesting combinatorial possibilities without detriment to the functionalization of amino acid side chains. These dimers represent a new class of self-assembling peptide nanotubes in which the hydrophobicity of the internal cavity (see picture) can be controlled.