Complexation of specific residues by carboxylatopillar[6]arene for improving the zymolytic stability of arginine-containing peptides

Longming Chen; Zhao Meng; Long Tian; Yahan Zhang; Liang Zhao; Xinbei Du; Mengke Ma; Han Zhang; Junyi Chen; Qingbin Meng

doi:10.1039/D2OB00017B

Complexation of specific residues by carboxylatopillar[6]arene for improving the zymolytic stability of arginine-containing peptides†

Longming Chen,‡^a Zhao Meng,‡^a Long Tian,^a Yahan Zhang,^a Liang Zhao,^a Xinbei Du,^a Mengke Ma,^a Han Zhang,^a Junyi Chen*^ab and Qingbin Meng

*^a

Author affiliations

* Corresponding authors

^a State Key Laboratory of Toxicology and Medical Countermeasures, Beijing Institute of Pharmacology and Toxicology, Beijing 100850, PR China
E-mail: naikaimqb@sina.com

^b Key Laboratory of Inorganic-Organic Hybrid Functional Material Chemistry, Ministry of Education, Tianjin Key Laboratory of Structure and Performance for Functional Molecules, College of Chemistry, Tianjin Normal University, Tianjin 300387, PR China
E-mail: jychen@tjnu.edu.cn

Abstract

A general strategy for improving the zymolytic stability against proteases is reported. Carboxylatopillar[6]arene (CP6A) could effectively bind arginine and arginine-containing peptides, thereby improving the stability of angiotensin peptides in the presence of trypsin by the complexation of the side chain of the arginine residue.

Organic & Biomolecular Chemistry

Complexation of specific residues by carboxylatopillar[6]arene for improving the zymolytic stability of arginine-containing peptides†

Abstract

Supplementary files

Article information

Download Citation

Permissions

Complexation of specific residues by carboxylatopillar[6]arene for improving the zymolytic stability of arginine-containing peptides

Social activity

Search articles by author

Spotlight

Advertisements