Porous Peptide Complexes by a Folding-and-Assembly Strategy.

Abstract

Concerted folding and assembly processes are necessary for protein self-assembly, yet such a concerted strategy has rarely been attempted by synthetic chemists. In this work, we have created a new porous peptide structure through a coordination-driven folding-and-assembly strategy. A porous framework with 1.5 nm-sized pores and a PII helical peptide scaffold was successfully obtained by complexation of AgNTf2 and tripeptide ligands containing the Gly-Pro-Pro sequence. The pores were modified in various ways with retention of the latent PII helical conformation of the peptide ligand.