Mapping the small molecule interactome by mass spectrometry.

Mapping the small molecule interactome by mass spectrometry.

Biochemistry. 2017 Oct 30;:

Authors: Flaxman HA, Woo CM

Abstract
Mapping small molecule interactions throughout the proteome provides the critical structural basis for functional analysis of their impact on biochemistry. However, translation of mass spectrometry-based proteomics methods to directly profile the interaction between a small molecule and the whole proteome is challenging due to the substoichiometric nature of many interactions, the diversity of covalent and noncovalent interactions involved, and the subsequent computational complexity associated with spectral assignment. Recent advances in mass spectrometry and chemical tools have begun to provide a structural basis for the breadth of small molecule-protein interactions in the whole proteome. Innovations enabling direct characterization of the small molecule interactome have centered on faster, more sensitive instrumentation coupled to chemical conjugation, enrichment, and labeling methods that facilitate detection and assignment. These methods have started to measure molecular interaction hot spots due to inherent differences in local amino acid reactivity and binding affinity throughout the proteome. Measurement of the small molecule interactome is producing structural insights into protein biochemistry that yields small molecule probes, therapeutic targets, and engineered modifications to the proteome. Direct structural characterization of the small molecule interactome is a rapidly emerging area that is producing new frontiers in biochemistry at the interface of small molecules and the proteome.

PMID: 29083874 [PubMed - as supplied by publisher]

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