DOI: https://doi.org/10.9767/bcrec.20617

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

1Department of Chemistry, National Dong Hwa University, Hualien 97403, Taiwan

2Research Center for Radiation Medicine, Chang Gung University, Taoyuan 33302, Taiwan

3Department of Neurology, Chang Gung Memorial Hospital, Taoyuan 33302, Taiwan

Received: 4 Jan 2026; Revised: 6 Feb 2026; Accepted: 7 Feb 2026; Available online: 4 Mar 2026; Published: 30 Aug 2026.
Editor(s): Istadi Istadi
Open Access Copyright (c) 2026 by Authors, Published by BCREC Publishing Group
Creative Commons License This work is licensed under a Creative Commons Attribution-ShareAlike 4.0 International License.
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Abstract

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).

Keywords: Acryloyl-amino acids; random copolymerization; mercaptoethanol; hydrolysis; Cbz- glycine ester
Funding: Taiwan National Science and Technology Council under contract NSTC 113-2314-B-182-055

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Section: Original Research Articles
Language : EN
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