Self-assembly approach to protein design

A small protein was self-assembled on a template. A metal-binding ligand, 4,4'-dicarboxylic acid-2,2'-bipyridine, was attached to the N-terminus of an oligopeptide with the potential to form an amphiphilic alpha -helix. These bipyridine-modified peptides trimerized to form a three alpha -helix bundle protein in the presence of FE(II). The cumulative binding constant was determined to be >5*1017 M-3, approximately 25 times greater than that of a control compound with no peptide moiety. Aldehyde templates are being developed to assemble unsymmetrical three alpha -helix bundle proteins.