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Updated: May 15, 2025

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Proteomimetic Strategy for the Modulation of Intrinsically Disordered Protein MYC.

Thu Nguyen¹, Seong Ho Hong¹, Paramjit Arora¹

¹Department of Chemistry, New York University, 100 Washington Square East, New York, New York 10003, United States.

Journal of the American Chemical Society

|April 8, 2025

Summary

This summary is machine-generated.

Designing drugs for dynamic proteins like MYC is challenging. This study developed a method to trap a specific protein shape, enabling the creation of targeted therapies for intrinsically disordered proteins.

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Area of Science:

Biochemistry
Structural Biology
Drug Discovery

Background:

Developing specific ligands for protein receptors is difficult, especially for conformationally dynamic and intrinsically disordered proteins (IDPs).
IDPs lack fixed structures, making it challenging to identify binding sites for synthetic ligand design.
MYC is a critical therapeutic target but has eluded small-molecule inhibitors due to its dynamic nature.

Purpose of the Study:

To develop a general method for designing ligands targeting intrinsically disordered proteins.
To demonstrate this approach using MYC, a known therapeutic target.

Main Methods:

Hypothesized that trapping a specific protein conformation could enable ligand design.
Designed a proteomimetic scaffold to capture the helical conformation of MYC when bound to MAX.
Validated the approach through biochemical and cellular assays.

Main Results:

Successfully designed a scaffold that traps the helical conformation of MYC.
Demonstrated that the designed scaffold can directly engage MYC.
Confirmed the utility of the approach in both in vitro and cellular settings.

Conclusions:

This work presents a generalizable strategy for targeting intrinsically disordered proteins.
The method involves trapping a specific, thermodynamically accessible conformation of the target protein.
This approach offers a promising avenue for developing therapeutics against challenging targets like MYC.