Minimalistic Artificial Catalysts with Esterase-Like Activity from Multivalent Nanofibers Formed by the Self-Assembly of Dipeptides

Ning Liu; Shuai-Bing Li; Yan-Zhen Zheng; Su-Ying Xu; Jiang-Shan Shen

doi:10.1021/acsomega.2c06972

Minimalistic Artificial Catalysts with Esterase-Like Activity from Multivalent Nanofibers Formed by the Self-Assembly of Dipeptides

ACS Omega. 2022 Dec 30;8(2):2491-2500. doi: 10.1021/acsomega.2c06972. eCollection 2023 Jan 17.

Authors

Ning Liu¹, Shuai-Bing Li¹, Yan-Zhen Zheng², Su-Ying Xu³, Jiang-Shan Shen¹

Affiliations

¹ Xiamen Key Laboratory of Optoelectronic Materials and Advanced Manufacturing, College of Materials Science and Engineering, Huaqiao University, Xiamen 361021, China.
² College of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China.
³ State Key Laboratory of Chemical Resource Engineering, Beijing Key Laboratory of Environmentally Harmful Chemical Analysis, Beijing University of Chemical Technology, Beijing 100029, China.

Abstract

Imitating and incorporating the multiple key structural features observed in natural enzymes into a minimalistic molecule to develop an artificial catalyst with outstanding catalytic efficiency is an attractive topic for chemists. Herein, we designed and synthesized one class of minimalistic dipeptide molecules containing a terminal -SH group and a terminal His-Phe dipeptide head linked by a hydrophobic alkyl chain with different lengths, marked as HS-C _n+1-His-Phe (n = 4, 7, 11, 15, and 17; n + 1 represents the carbon atom number of the alkyl chain). The His (-imidazole), Phe (-CO₂ ^-) moieties, the terminal -SH group, and a long hydrophobic alkyl chain were found to have important contributions to achieve high binding ability leading to outstanding absolute catalytic efficiency (k _cat/K _M) toward the hydrolysis reactions of carboxylic ester substrates.