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Privileged Substructures to Modulate Protein-Protein Interactions.

Nicolas Bosc1,2,3,4, Mélaine A Kuenemann1,2, Jerome Bécot1,2

  • 1Inserm, U973 , Paris 75013, France.

Journal of Chemical Information and Modeling
|September 19, 2017
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Summary
This summary is machine-generated.

Identifying effective chemical probes for modulating protein-protein interactions (PPIs) is challenging. This study reveals privileged chemical scaffolds and moieties crucial for designing potent and safe PPI inhibitors, aiding drug discovery efforts.

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Area of Science:

  • Medicinal Chemistry
  • Chemical Biology
  • Drug Discovery

Background:

  • Identifying chemical probes to modulate protein-protein interactions (PPIs) presents significant challenges.
  • The development of PPI-tailored screening collections is recognized as essential, yet the specific scaffolds promoting compound binding to PPI targets remain unclear.

Purpose of the Study:

  • To identify privileged chemical substructures frequently found in inhibitors of protein-protein interactions (PPIs).
  • To provide chemical guidance for medicinal chemists in discovering high-quality chemical probes for PPI targets.

Main Methods:

  • Utilized big data analysis to identify frequently occurring chemical substructures in PPI inhibitors.
  • Employed molecular frameworks to analyze chemical substructures within experimental and machine-learning predicted datasets of inhibitors of PPIs (iPPIs).

Main Results:

  • A list of privileged chemical substructures, including scaffolds and moieties, was identified.
  • These substructures are suitable for chemical functionalization and are free from toxicophores and pan-assay interference (PAINS) alerts.

Conclusions:

  • The identified privileged substructures offer valuable guidance for medicinal chemists.
  • This guidance facilitates the rational design and discovery of novel chemical probes targeting PPIs.