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Ester Bond: Chemically Labile Yet Mechanically Stable

ACS Nano. 2023-08; 
Hai Lei, Quan Ma, Zhangxia Wang, Di Zhang, Xiaoyu Huang, Meng Qin, Haibo Ma, Wei Wang, Yi Cao
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Abstract

Due to the dynamic nature of ester linkages, ester-bond-containing materials are well known for their outstanding degradability and stimuli responsiveness. However, whether ester hydrolysis is affected by mechanical forces remains unclear. Here, we develop a single-molecule assay to quantitatively study the force-dependent ester hydrolysis using an engineered circular permutant protein with a caged ester bond as a model. Our single-molecule force spectroscopy results show that the ester hydrolysis rate is surprisingly insensitive to forces, with a ∼7 s dissociation rate that remains almost unchanged in the force range of 80 to 200 pN. Quantum calculations reveal that the ester hydrolysis involves an intermedi... More

Keywords

atomic force microscopy, ester bond, hydrolysis, mechanical force, protein unfolding, single-molecule force spectroscopy