Nature communications | VOL. 13
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Native metabolomics identifies the rivulariapeptolide family of protease inhibitors

Publication Date Aug 8, 2022

Abstract

The identity and biological activity of most metabolites still remain unknown. A bottleneck in the exploration of metabolite structures and pharmaceutical activities is the compound purification needed for bioactivity assignments and downstream structure elucidation. To enable bioactivity-focused compound identification from complex mixtures, we develop a scalable native metabolomics approach that integrates non-targeted liquid chromatography tandem mass spectrometry and detection of protein binding via native mass spectrometry. A native metabolomics screen for protease inhibitors from an environmental cyanobacteria community reveals 30 chymotrypsin-binding cyclodepsipeptides. Guided by the native metabolomics results, we select and purify five of these compounds for full structure elucidation via tandem mass spectrometry, chemical derivatization, and nuclear magnetic resonance spectroscopy as well as evaluation of their biological activities. These results identify rivulariapeptolides as a family of serine protease inhibitors with nanomolar potency, highlighting native metabolomics as a\xa0promising approach for drug discovery, chemical ecology, and chemical biology studies.

Concepts

Family Of Serine Protease Inhibitors Family Of Protease Inhibitors Native Mass Spectrometry Liquid Chromatography Tandem Mass Spectrometry Protease Inhibitors Family Of Inhibitors Nanomolar Potency Nuclear Magnetic Resonance Spectroscopy Chemical Ecology Chemical Derivatization

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