Engineering β‑Sheet Peptide Coassemblies for Biomaterial Applications

• Published in: The journal of physical chemistry. B Vol. 125; no. 50; pp. 13599 - 13609
• Main Authors: Wong, Kong M, Robang, Alicia S, Lint, Annabelle H, Wang, Yiming, Dong, Xin, Xiao, Xingqing, Seroski, Dillon T, Liu, Renjie, Shao, Qing, Hudalla, Gregory A, Hall, Carol K, Paravastu, Anant K
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 23.12.2021
• Subjects: Biocompatible Materials; Magnetic Resonance Spectroscopy; Nanostructures; Peptides; Protein Conformation, beta-Strand
• ISSN: 1520-6106; 1520-5207
• DOI: 10.1021/acs.jpcb.1c04873

Peptide coassembly, wherein at least two different peptides interact to form multicomponent nanostructures, is an attractive approach for generating functional biomaterials. Current efforts seek to design pairs of peptides, A and B, that form nanostructures (e.g., β-sheets with ABABA-type β-strand patterning) while resisting self-assembly (e.g., AAAAA-type or BBBBB-type β-sheets). To confer coassembly behavior, most existing designs have been based on highly charged variants of known self-assembling peptides; like-charge repulsion limits self-assembly while opposite-charge attraction promotes coassembly. Recent analyses using solid-state NMR and coarse-grained simulations reveal that preconceived notions of structure and molecular organization are not always correct. This perspective highlights recent advances and key challenges to understanding and controlling peptide coassembly.