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Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

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Method for Identifying Small Molecule Inhibitors of the Protein-protein Interaction Between HCN1 and TRIP8b

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Targeting the hSSB1-INTS3 Interface: A Computational Screening Driven Approach to Identify Potential Modulators.

Tabassum Khair Barbhuiya^1,2, Sam Beard^2,3, Esha T Shah^2,3

¹Centre for Genomics and Personalised Health, and School of Chemistry and Physics, Faculty of Science, Queensland University of Technology, 2 George Street, Brisbane, QLD 4000, Australia.

|February 26, 2024

Summary

This summary is machine-generated.

Researchers identified novel compounds that disrupt the interaction between human single-stranded DNA binding protein 1 (hSSB1) and INTS3. This finding offers a new strategy for targeting cancer by inhibiting DNA repair pathways.

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Area of Science:

Molecular Biology
Structural Biology
Cancer Research

Background:

Human single-stranded DNA binding protein 1 (hSSB1) is crucial for DNA repair, forming the SOSS1 complex with INTS3 and C9ORF80.
Elevated hSSB1 activity in cancers suggests its potential as an anticancer therapeutic target.
Previous inhibition strategies focused on hSSB1's DNA binding domain, with limited success.

Purpose of the Study:

To investigate the inhibition of hSSB1 function by disrupting its interaction with INTS3 within the SOSS1 complex.
To identify drug-like compounds that can impede the INTS3-hSSB1 protein-protein interaction (PPI).

Main Methods:

Molecular docking screening of a compound library against the INTS3 protein at the hSSB1 binding interface.
In vitro assessment of PPI disruption using co-immunoprecipitation assays.
Cellular effect evaluation via immunofluorescence assays and chromatin recruitment studies.
Molecular dynamics simulations to assess ligand binding stability at the INTS3 hot-spot site.

Main Results:

Three compounds demonstrated potential in vitro disruption of the INTS3-hSSB1 interaction.
One compound significantly impacted the recruitment of hSSB1 and INTS3 to chromatin after DNA damage.
This study presents the first drug-like compounds targeting the INTS3-hSSB1 interaction.

Conclusions:

Disrupting the INTS3-hSSB1 interaction represents a novel therapeutic strategy for cancer treatment.
The identified compounds provide a foundation for further biophysical studies and PPI inhibitor development.
Targeting protein-protein interactions in DNA repair pathways offers promising avenues for anticancer drug discovery.