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Novel RNA-Binding Proteins Isolation by the RaPID Methodology

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mRNA Display Identifies Potent, Paralog-Selective Peptidic Ligands for ARID1B.

Gregor S Cremosnik¹, Yannick Mesrouze², Patrik Zueger¹

¹Global Discovery Chemistry, Novartis Biomedical Research, CH-4056 Basel, Switzerland.

ACS Chemical Biology

|April 24, 2024

Summary

This summary is machine-generated.

Researchers identified ARID1B-selective peptides, offering new cancer drug targets. These peptides bind ARID1B, a paralog of ARID1A, crucial for cancer cell growth when ARID1A is mutated.

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Area of Science:

Chromatin remodeling complexes
Cancer biology
Drug discovery

Background:

ARID1A and ARID1B are subunits of SWI/SNF chromatin remodeling complexes.
ARID1A mutations are common in cancer, leading to ARID1B dependency for proliferation.
ARID1B remains an untargeted paralog due to high sequence similarity with ARID1A.

Purpose of the Study:

To identify selective ligands for ARID1B.
To explore ARID1B as a potential drug target.
To investigate the synthetic lethal relationship between ARID1A and ARID1B in cancer.

Main Methods:

Utilized mRNA display to discover peptidic ligands.
Employed biochemical, biophysical, and chemical biology techniques for validation.
Assessed binding affinity and selectivity against ARID1A.

Main Results:

Identified peptidic ligands with nanomolar affinity for ARID1B.
Demonstrated high selectivity of these peptides for ARID1B over ARID1A.
Characterized peptide binding to two distinct pockets, including an ARID1B-exclusive cysteine.

Conclusions:

ARID1B is a 'ligandable' target, validated by selective peptide binders.
The identified peptides serve as valuable tools for drug discovery.
Findings suggest opportunities for developing selective molecules targeting ARID1B for cancer therapy.