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Mass Spectrometry Reveals the Direct Action of a Chemical Chaperone. | LitMetric

Mass Spectrometry Reveals the Direct Action of a Chemical Chaperone.

J Phys Chem Lett

Science for Life Laboratory, Department of Microbiology, Tumor and Cell Biology , Karolinska Institutet, Tomtebodavägen 23A , 171 65 Stockholm , Sweden.

Published: July 2018

AI Article Synopsis

Article Abstract

Despite their fundamental biological importance and therapeutic potential, the interactions between chemical chaperones and proteins remain difficult to capture due to their transient and nonspecific nature. Using a simple mass spectrometric assay, we are able to follow the interactions between proteins and the chemical chaperone trimethylamine- N-oxide (TMAO). In this manner, we directly observe that the counteraction of TMAO and the denaturant urea is driven by the exclusion of TMAO from the protein surface, whereas the surfactant lauryl dimethylamine- N-oxide cannot be displaced. Our results clearly demonstrate a direct chaperoning mechanism for TMAO, corroborating extensive computational studies, and pave the way for the use of nondenaturing mass spectrometry and related techniques to study chemical chaperones in molecular detail.

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http://dx.doi.org/10.1021/acs.jpclett.8b01817DOI Listing

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