Design of Ferrocene-Dipeptide Bioorganometallic Conjugates To Induce Chirality-Organized Structures

摘要

Tnhe highly ordered molecular assemblies in pro-nteins can have a variety of functions, asnobserved in enzymes, receptors, and the like. Syn-nthetic scientists are constructing bioinspired sys-ntems by harnessing the self-assembling propertiesnof short peptides. Secondary structures such asn-helices, u0001-sheets, and u0001-turns are important innprotein folding, which is mostly directed and sta-nbilized by hydrogen bonding and the hydropho-nbic interactions of side chains. The design of secondary structure mimics that are composed of short peptides has attractednmuch attention, both for gaining fundamental insight into the factors affecting protein folding and for developing pharma-ncologically useful compounds, artificial receptors, asymmetric catalysts, and new materials.nFerrocenes are an organometallic scaffold with a central reverse-turn unit based on the inter-ring spacing of about 3.3nÅ, which is a suitable distance for hydrogen bonding between attached peptide strands. The conjugation of organometallicncompounds with biomolecules such as amino acids, peptides, and DNA should provide novel systems that reflect proper-nties of both the ferrocene and the biologically derived moieties. In this Account, we focus on recent advances in the designnof ferrocene peptide bioconjugates, which help illustrate the peptidomimetic basis for protein folding and the means ofnconstructing highly ordered molecular assemblies.