Secondary Structures in Synthetic Poly(Amino Acids): Homo‐ and Copolymers of Poly(Aib), Poly(Glu), and Poly(Asp)

• Published in: Macromolecular bioscience Vol. 23; no. 4; pp. e2200344 - n/a
• Main Authors: Rohmer, Matthias, Freudenberg, Jan, Binder, Wolfgang Hubertus
• Format: Journal Article
• Language: English
• Published: Germany Wiley Subscription Services, Inc 01.04.2023
• Subjects: 2‐aminoisobutyric acid; Amino acids; Amino Acids - chemistry; Amyloid; Aspartic acid; Biomolecules; Copolymers; Fibrillation; Folding; Glutamic acid; Glutamic Acid - chemistry; hybrid materials; poly(amino acids); Polymers; Protein folding; Protein structure; Protein Structure, Secondary; Proteins; Secondary structure; secondary structures; Supramolecular polymers; glutamic acid; poly(amino acids); hybrid materials; aspartic acid; secondary structures; 2-aminoisobutyric acid
• ISSN: 1616-5187; 1616-5195; 1616-5195
• DOI: 10.1002/mabi.202200344

The secondary structure of poly(amino acids) is an excellent tool for controlling and understanding the functionality and properties of proteins. In this perspective article the secondary structures of the homopolymers of oligo‐ and poly‐glutamic acid (Glu), aspartic acid (Asp), and α‐aminoisobutyric acid (Aib) are discussed. Information on external and internal factors, such as the nature of side groups, interactions with solvents and interactions between chains is reviewed. A special focus is directed on the folding in hybrid‐polymers consisting of oligo(amino acids) and synthetic polymers. Being part of the SFB TRR 102 “Polymers under multiple constraints: restricted and controlled molecular order and mobility” this overview is embedded into the cross section of protein fibrillation and supramolecular polymers. As polymer‐ and amino acid folding is an important step for the utilization and design of future biomolecules these principles guide to a deeper understanding of amyloid fibrillation. Poly(amino acids) allow to study the assembly and function of proteins. The folding and aggregation of oligo‐ and poly‐glutamic acids, aspartic acids and α‐aminoisobutyric acids and the impact of solvents and functional groups is reviewed. Embedded at the cross‐section of protein fibrillation and supramolecular polymers, these molecules allow the future design of functional biomaterials, guiding further into amyloid fibrillation.