Functionality of Polypeptide by Induction of Specific Tertiary Structure

Abstract

Regular assemblies of peptide molecules to exhibit novel functionalities have been prepared in two different ways. One of them is a helix-bundle structure in which two or three hydrophobic α-helical peptides are connected together by a tie molecule. The helix-bundle structure formed an ion channel across lipid bilayer membrane at lower concentrations than a single-chain pepide. The other example is a two-dimensional assembly of amphiphilic peptide molecules carrying a chromophoric group. The assembly was an efficient photo-energy collector to generate photo-electron and to reduce cytochrome c.