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Issue 63, 2018
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Chemoenzymatic synthesis of polypeptides in neat 1,1,1,2-tetrafluoroethane solvent

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Abstract

Chemoenzymatic polypeptide synthesis offers several advantages over chemical or other biological routes, however, the use of aqueous-based media suffers from reverse hydrolysis reactions that challenge peptide chain propagation. Herein, the protease from subtilisin Carlsberg biocatalyzed the synthesis of poly-L-PheOEt, poly-L-LeuOEt, and the copolymers poly-L-PheOEt-co-L-LeuOEt from their amino acid ethyl ester substrates in a neat liquid 1,1,1,2-tetrafluoroethane solvent. The products, achieved in acceptable yields (ca. 50%), were fully characterized showing relatively high molar mass (ca. 20 000 Da for poly-L-PheOEt). This non-toxic low-boiling hydrofluorocarbon enhances enzymatic peptide propagation by limiting hydrolysis owing to its hydrophobic and relatively polar characteristics that sustain the protease activity and solubilize substrates and products. Computational molecular dynamic calculations were used to assess the L-PheOEt/L-LeuOEt-solvent and polypeptide-solvent interactions in this system. Additionally, the homopolypeptides displayed higher crystallinity than the copolypeptides with random incorporation of amino acid ethyl esters, notwithstanding the significantly highest specificity for Phe in this system. Interestingly, secondary structure characterization of the products by FTIR and circular dichroism suggests a non-common peptide folding.

Graphical abstract: Chemoenzymatic synthesis of polypeptides in neat 1,1,1,2-tetrafluoroethane solvent

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Supplementary files

Article information


Submitted
07 Aug 2018
Accepted
17 Oct 2018
First published
22 Oct 2018

This article is Open Access

RSC Adv., 2018,8, 35936-35945
Article type
Paper

Chemoenzymatic synthesis of polypeptides in neat 1,1,1,2-tetrafluoroethane solvent

I. S. Aguirre-Díaz, C. Montiel, I. Bustos-Jaimes, Y. Medina-Gonzalez, A. Tecante and M. Gimeno, RSC Adv., 2018, 8, 35936
DOI: 10.1039/C8RA06657D

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