Targeting Protein-Protein Interaction with Covalent Small-Molecule Inhibitors.

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2019
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Abstract
PPIs are involved in diverse biochemical events and perform their functions through the formation of protein-protein complexes or PPI networks. The large and flat interacting surfaces of PPIs make discovery of small-molecule modulators a challenging task. New strategies and more effective chemical technologies are needed to facilitate the development of PPIs small-molecule inhibitors. Covalent modification of a nucleophilic residue located proximally to the immediate vicinity of PPIs can overcome the disadvantages of large interacting surfaces and provides high-affinity inhibitors with increased duration of action and prolonged target modulation. On the other hand, covalent inhibitors that target non-conserved protein residues demonstrate improved selectivity over related protein family members. Herein, we highlight the latest progress of small-molecule covalent PPIs inhibitors and hope to shed light on future PPIs inhibitor design and development. The relevant challenges and opportunities are also discussed.
Reference Key
li2019targetingcurrent Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Li, Bingbing;Rong, Deqin;Wang, Yuanxiang;
Journal Current topics in medicinal chemistry
Year 2019
DOI
10.2174/1568026619666191011163410
URL
Keywords
gpcr protein-protein interaction cysteine covalent inhibitor lysine methionine.

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