Chemoenzymatic synthesis of polypeptides consisting of periodic di- and tri-peptide motifs similar to elastin. Issue 17 (17th April 2018)

• Record Type: Journal Article
• Authors: Gudeangadi, Prashant G.; Tsuchiya, Kousuke; Sakai, Takamasa; Numata, Keiji
• Is Part Of: Polymer chemistry. Volume 9:Issue 17(2018)
• Page Start: 2336
• Page End: 2344
• Publication Date: 2018-04-17
• Subjects: Polymers -- Periodicals; Macromolecules -- Periodicals; Polymerization -- Periodicals; 547.705
• DOI: 10.1039/c8py00034d
• Languages: English
• ISSNs: 1759-9954

Abstract

Abstract : Elastin-like polypeptides containing proline were synthesized via chemoenzymatic polymerization and exhibited a temperature-dependent structural transition. 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.