Protease-catalyzed enzymatic synthesis of antifreeze peptide oligomers and their cryopreservation performance.

ABSTRACT: Sub-zero preservation is essential in biomedical fields like tissue engineering, gene therapy, and transplantation. Traditional cryoprotectants like dimethyl sulfoxide are toxic and can alter cell epigenetics, necessitating safer alternatives. Herein, an enzymatic synthesis of antifreeze peptide oligomers (AFPOs) using protease-catalyzed polymerization is introduced. Employing proteases as catalysts, AFPOs were synthesized by condensing L-alanyl-alanyl-threonine (L-AAT) as a model monomer, and this method was extended to produce two additional sequences, poly(L-alanyl-threonine-alanyl) (L-PATA) and poly(L-threonine-alanyl-alanyl) (L-PTAA). Notably, using L-alanyl-threonyl-alanine (L-ATA) as the monomer, a degree of polymerization up t

SUBMITTER: Pan X 

PROVIDER: S-EPMC12651731 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature