Mapping the Small Molecule Interactome by Mass Spectrometry

Biochemistry
Hope A Flaxman, Christina M Woo

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 because of the substoichiometric nature of many interactions, the diversity of covalent and noncovalent interactions involved, and the subsequent computational complexity associated with their spectral assignment. Recent advances in chemical proteomics have begun fill this gap 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 include 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 hotspots 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 and methods for probing and engineering protein bioc...Continue Reading

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Citations

Apr 28, 2018·High-throughput·Vehary Sakanyan
Oct 22, 2020·Chemical Communications : Chem Comm·Fan Yang, Chu Wang
Dec 23, 2020·Chembiochem : a European Journal of Chemical Biology·Abdallah S AbdelsattarFareed Aboul-Ela
Jan 14, 2020·Bioconjugate Chemistry·Ivan BassaniniSergio Romeo

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