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Updated: Sep 13, 2025

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function
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A Charge-Driven Strategy for Covalent Modification and Modulation of Biomolecular Condensates.

Zhewei Chen1, Lu Liu1, Jerome Cattin2

  • 1Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Journal of the American Chemical Society
|August 2, 2025
PubMed
Summary
This summary is machine-generated.

Researchers developed a new charge-driven strategy to inhibit biomolecular condensate formation, targeting Ras GTPase-activating protein-binding protein 1 (G3BP1) to prevent stress granule assembly, offering a novel therapeutic approach.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Chemical Biology

Background:

  • Biomolecular condensates are crucial cellular structures implicated in diseases like neurodegeneration and cancer.
  • Directly targeting proteins that mediate condensate formation with small molecules is challenging.
  • Ras GTPase-activating protein-binding protein 1 (G3BP1) is a key protein in stress granule (SG) formation.

Purpose of the Study:

  • To present a novel charge-driven strategy for modulating biomolecular condensate formation.
  • To demonstrate the application of this strategy in inhibiting G3BP1-mediated stress granule formation.
  • To explore the mechanism of action for small-molecule inhibitors targeting G3BP1.

Main Methods:

  • Development of small-molecule SG inhibitors using a carbonylacrylic amide covalent functionality.
  • Modification of the folded domain of G3BP1 to introduce surface charges.
  • Utilizing cellular experiments with HeLa cells expressing cysteine-mutated G3BP1.
  • Conducting structure-activity relationship studies and molecular dynamics simulations.

Main Results:

  • The small-molecule modification of G3BP1 altered conformational dynamics of intrinsically disordered regions.
  • Cellular experiments and SAR studies supported the proposed charge-driven mechanism.
  • Molecular dynamics simulations indicated a shift towards more compact G3BP1 conformations.

Conclusions:

  • Established a novel charge-driven strategy for the rational modulation of biomolecular condensates.
  • Demonstrated the potential of this strategy to inhibit G3BP1-mediated stress granule formation.
  • Provided insights into the conformational changes induced by small-molecule G3BP1 modification.