Tuning the conformation of synthetic co-polypeptides of serine and glutamic acid through control over polymer composition
| Autor: | Arianna Pasquazi, Jonathan W. Aylott, Mwm Martin Fijten, Lee D.K. Buttery, Anne Canning, Mischa Zelzer, Sunil Rajput |
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| Rok vydání: | 2016 |
| Předmět: |
polypeptides
Polymers and Plastics Stereochemistry Dispersity 02 engineering and technology 010402 general chemistry 01 natural sciences Ring-opening polymerization Polymer chemistry Materials Chemistry Copolymer Protein secondary structure Peptide sequence chemistry.chemical_classification Organic Chemistry conformational analysis copolymerization kinetics secondary structure structure-property relations Polymer 021001 nanoscience & nanotechnology 0104 chemical sciences Amino acid N-carboxy anhydride (NCA) polymerization chemistry Polymerization 0210 nano-technology |
| Zdroj: | Journal of Polymer Science, Part A: Polymer Chemistry, 54(15), 2331-2336. Wiley |
| ISSN: | 0887-624X |
| Popis: | Ring opening polymerization (ROP) of N-carboxy anhydride (NCA) amino acids presents a rapid way to synthesize high molecular weight polypeptides with different amino acid compositions. The compositional and functional versatility of polypeptides make these materials an attractive choice for biomaterials. The functional performance of polypeptide materials is equally linked to their conformation which is determined by the amino acid sequence in the polymer chains. Here, the interplay between composition and conformation of synthetic polypeptides obtained by NCA polymerization was explored. Various copolypeptides from Glu(Bzl) and Ser(Bzl) were prepared to investigate how polypeptide composition affected the conformation of the resulting copolymer. Polymerization kinetics indicated that the copolymerization of Glu(Bzl) and Ser(Bzl) preferentially yielded alternating copolymers. Both the polydispersity and the conformation of the polypeptides were dependent on the Ser(Bzl) content in the polymer, demonstrating that polypeptide functionalities could be tuned directly by altering the relative amounts of amino acids in the chain. This work presents the first step toward an improved understanding and control over polypeptide conformation through modulating the amino acid composition of the material. Understanding this sequence–functionality relationship is essential to advancing the use of ROP as a technique to design smart polypeptide based materials with specific functions. © 2016 The Authors. Journal of Polymer Science Part A: Polymer Chemistry Published by Wiley Periodicals, Inc. J. Polym. Sci., Part A: Polym. Chem. 2016, 54, 2331–2336 |
| Databáze: | OpenAIRE |
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