Constructing the Active Sites of an Artificial Hydrolase Using Mercaptoethanol as a Destructive Agent

Dar-Fu Tai (Department of Chemistry, National Dong Hwa University, Hualien 97403)
Sue-Chen Wang (Department of Chemistry, National Dong Hwa University, Hualien 97403)
Lisa Chen (Department of Chemistry, National Dong Hwa University, Hualien 97403)
Venkatachalam Angamuthu (Department of Chemistry, National Dong Hwa University, Hualien 97403)
Chung-Yin Lin (Research Center for Radiation Medicine, Chang Gung University, Taoyuan 33302||Taiwan Department of Neurology, Chang Gung Memorial Hospital, Taoyuan 33302)

Bulletin of Chemical Reaction Engineering & Catalysis
2026: BCREC Volume 21 Issue 2 Year 2026 (August 2026)

In the present study, (N-acryloyl-L-cysteine-benzyl amide)2 (Acryl-L-Cys-NHBn)2, N-acryloyl-L-histidine-benzyl amide (Acryl-L-His-NHBn), and N-acryloyl-aspartic acid-benzyl amide (Acryl-L-Asp-NHBn) were chemo-enzymatically synthesized from Boc-L-amino acids. Then, a mixture of these acryl amino acid monomers was copolymerized to form polymers. The resulting random polymers were then activated after a mercaptoethanol-triggered reduction of disulfide linkages to thiol. The activated polymer demonstrated substrate selectivity, turnover, and rate enhancement in catalyzing the hydrolysis of the esters of Cbz-glycine. The results demonstrated that radical polymerization can facilitate the task of preparing synthetic macromolecules capable of enzyme-like catalytic turnover, substrate selectivity, and rate enhancement. Copyright © 2026 by Authors, Published by BCREC Publishing Group. This is an open access article under the CC BY-SA License (https://creativecommons.org/licenses/by-sa/4.0).