Covalent Capture and Stabilization of Cylindricalβ-Sheet Peptide Assemblies

Abstract

Covalent capture of supramolecular peptide assemblies such as A leads to kinetically stable cylindrical β-sheet structures B. The covalent bond-forming processes employed must be mild enough to tolerate peptide backbone groups as well as intersubunit hydrogen bonding. On the basis of these criteria, olefin metathesis using a selective RuII catalyst developed by Grubbs et al. as well as cysteine disulfide formation were investigated. This general strategy involving the marriage of noncovalent and covalent chemistry may prove useful in preparation of functional molecular constructs.