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Related Concept Videos

Protein-protein Interfaces02:04

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 polypeptide...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Discovery and Biological Characterization of PRMT5:MEP50 Protein-Protein Interaction Inhibitors.

Andrew M Asberry1,2, Xinpei Cai3, Xuehong Deng1

  • 1Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, Indiana 47907, United States.

Journal of Medicinal Chemistry
|October 7, 2022
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Researchers developed compound 17, a novel inhibitor targeting the Protein Arginine Methyltransferase 5:Methylosome Protein 50 (PRMT5:MEP50) protein-protein interaction. This approach offers a new strategy for cancer therapy by disrupting essential epigenetic regulation.

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Area of Science:

  • Epigenetics
  • Chemical Biology
  • Cancer Therapeutics

Background:

  • Protein arginine methyltransferase 5 (PRMT5) is a key epigenetic regulator and a validated cancer target.
  • PRMT5 function relies on its obligate cofactor, methylosome protein 50 (MEP50).
  • Targeting the PRMT5:MEP50 interaction presents a novel therapeutic strategy.

Purpose of the Study:

  • To develop and characterize a small-molecule inhibitor targeting the PRMT5:MEP50 protein-protein interaction (PPI).
  • To evaluate the compound's efficacy and mechanism of action in cancer cells.

Main Methods:

  • Virtual screening and analogue refinement to identify compound 17.
  • Molecular docking to predict the binding mode.
  • In vitro assays to assess inhibition of PRMT5:MEP50 activity and gene expression.
  • RNA-sequencing (RNA-seq) to analyze downstream signaling pathways.

Main Results:

  • Compound 17 selectively inhibits the PRMT5:MEP50 PPI with IC50 < 500 nM in prostate and lung cancer cells.
  • Specific inhibition of PRMT5:MEP50 substrate methylation and target gene expression was observed.
  • RNA-seq data suggest compound 17 may dysregulate TGF-β signaling.

Conclusions:

  • Compound 17 serves as a proof-of-concept for targeting the PRMT5:MEP50 PPI.
  • This PPI inhibition represents a novel mechanism of action distinct from catalytic inhibition.
  • Further preclinical development of PRMT5:MEP50 PPI inhibitors is warranted.