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

Abstract

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.

A Living Topochemical Ring‐Opening Polymerization of Achiral Amino Acid N‐Carboxy‐Anhydrides in Single Crystals

“…The largest signals in all spectra could be assigned to poly(Aib) bearing the initiator at the C‐terminus and a hydrogen at the N‐terminus ionized with a sodium ion [C 10 H 12 N(C 4 H 7 NO) n H+Na] + . In order to compare the outcome of the topochemical ROP to those of a conventional solution ROP, we conducted the same ROP also in solution under known conditions, as reported by us recently [21a,23] . MALDI‐ToF MS of the solution polymerization (Figure 2C, D) shows multiple side reactions occurring during the polymerization with an only limited molecular weight (n=32) due to the poor solubility of the final polymer.…”

Antifouling polymers for nanomedicine and surfaces: recent advances

“…Poly(amino acids) (PAAs) is another class of hydrophilic antifouling polymers that has shown promise for nanomedicine applications due to their biocompatibility, biodegradability, and tunable physicochemical properties. [72][73][74][75][76][77][78] PAAs are formed by linking amino acids together through peptide bonds, and the sidechains can be custom designed to contain different functional groups, including amino, carboxylic acid, and thiol groups. This makes PAAs highly versatile as their properties can be rationally engineered and fine-tuned based on the functional groups present, which in turn enables interaction/conjugation with drugs, targeting agents, and other active agents for biomedical applications.…”

Protein‐Inspired Control over Synthetic Polymer Folding for Structured Functional Nanoparticles in Water

“…We focus in this review on fully synthetic systems that collapse/fold into compartmentalized structures in water, to facilitate the comparison to proteins, but note that many elegant examples of conformational control have been attained in organic solvents, which have been reviewed elsewhere. [2][3][4][5][6][7][8][9] In addition, elegant work conducted in the fields of synthetic peptides [10] and protein/peptide-polymer hybrids [11,12] has been reviewed elsewhere and will not be part of this review. A particularly interesting class of synthetic polymers for which control over their 3D structure has been explored are the amphiphilic heterograft polymers (AHPs) -polymer chains with randomly distributed, different types of grafts.…”