Chapter 7 - Hybrid Systems Engineering: Polymer–Peptide Conjugates

Abstract

Peptide–polymer copolymers represent a promising approach to utilizing the self-assembling behaviors of peptides to direct the nanoscale organization of synthetic polymers. Two main structural motifs allow the complex, hierarchical organization of peptide sequences: β-sheets and α-helices. Experience to date suggests that the conjugation of random coil amphiphilic synthetic polymers to peptide sequences does not significantly interfere with the supramolecular self-assembly of the peptides. Commonly, peptide–polymer copolymers self-assemble into a peptide core, surrounded by a polymer shell, and the latter can thereby prevent uncontrolled lateral aggregation of the peptides. A number of common conjugation approaches are described. Amine coupling to lysine residues via N -hydroxy succinimide functionalization of the polymer is a convenient but nonspecific method of conjugation. Maleimide coupling to a free cysteine residue is the most common method for site-specific conjugation. Polymers can be attached either within or at the ends of peptide sequences, providing control of the molecular conformation. Examples of peptide–polymer self-assembly are given to demonstrate the range of conformations that can be synthesized.