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Chemoenzymatic synthesis of polypeptides consisting of periodic di- and tri-peptide motifs similar to elastin

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Abstract

Proline and valine exist in repetitive motifs in various structural proteins and play an important role in their physiological functions. Herein, we synthesized polypeptides that consist of di- and tri-peptide motifs containing proline and valine via chemoenzymatic polymerization. Di- and tri-peptide ethyl esters (ValGly-OEt, GlyProGly-OEt, and ValProGly-OEt) could be polymerized by papain, whereas proline and valine ethyl esters (Pro-OEt, Val-OEt) were inactive in chemoenzymatic polymerization because of their poor affinity for papain. The copolymer of ValProGly-OEt and ValGly-OEt being poly(ValProGly-co-ValGly), which is composed of a repetitive sequence of elastin, exhibited a temperature-dependent structural transition similar to tropoelastin. The post-polycondensation product of poly(ValProGly-co-ValGly) showed higher molecular weight and elastin-like thermal behaviors.

Graphical abstract: Chemoenzymatic synthesis of polypeptides consisting of periodic di- and tri-peptide motifs similar to elastin

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Publication details

The article was received on 09 Jan 2018, accepted on 17 Mar 2018 and first published on 17 Apr 2018


Article type: Paper
DOI: 10.1039/C8PY00034D
Citation: Polym. Chem., 2018, Advance Article
  • Open access: Creative Commons BY license
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    Chemoenzymatic synthesis of polypeptides consisting of periodic di- and tri-peptide motifs similar to elastin

    P. G. Gudeangadi, K. Tsuchiya, T. Sakai and K. Numata, Polym. Chem., 2018, Advance Article , DOI: 10.1039/C8PY00034D

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