Micelle-modulated reactivity of novel copper(<scp>ii</scp>) complexes with reduced <scp>l</scp>-histidine Schiff bases as mimic carboxylesterases-Reference-Cited by-同舟云学术

Micelle-modulated reactivity of novel copper(ii) complexes with reduced l-histidine Schiff bases as mimic carboxylesterases

Published:2024 Issue:18 Volume:48 Page:8445-8453
ISSN:1144-0546
Container-title:New Journal of Chemistry
language:en
Short-container-title:New J. Chem.

Author:

Ni Tong¹,Zhang Qin²,Wang Xiuyang¹,Xu Bin¹,Zhou Shengbin¹,Zhang Kaiming¹,Jiang Weidong¹^ORCID

Affiliation:

1. School of Chemistry and Environmental Engineering, Key Laboratory of Green Chemistry of Sichuan Institutes of Higher Education, Sichuan University of Science & Engineering, Sichuan Zigong 643000, P. R. China

2. Small Molecule Division, Porton Pharma Solutions Ltd., Chongqing Beibei 400700, P. R. China

Abstract

Various micelles provided distinguishable effects on the catalytic performance of novel copper(ii) complexes (1 and 2) with reduced l-histidine Schiff bases towards hydrolytic cleavage of PNPA.

Funder

National Natural Science Foundation of China

Sichuan University of Science and Engineering

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/NJ/D4NJ00486H

Reference56 articles.

1. Feruloyl esterase immobilization in mesoporous silica particles and characterization in hydrolysis and transesterification

2. Detection techniques of carboxylesterase activity: An update review

3. Ethyl butanoate is synthesised both by alcoholysis and esterification by dairy lactobacilli and propionibacteria

4. Characterization of the metabolism of eupalinolide A and B by carboxylesterase and cytochrome P450 in human liver microsomes

5. Carboxylesterase 1 and Precision Pharmacotherapy: Pharmacogenetics and Nongenetic Regulators