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

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 pola

SUBMITTER: Aguirre-Diaz IS 

PROVIDER: S-EPMC9088702 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature