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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Rapid Identification of Pathogens01:25

Rapid Identification of Pathogens

MALDI-TOF MS has transformed clinical microbiology by offering a rapid and reliable method for pathogen identification. The traditional approach to microbial identification typically involves time-consuming culture techniques and biochemical tests, which can delay the initiation of appropriate antimicrobial therapy. MALDI-TOF MS avoids these delays by using characteristic ribosomal protein mass patterns of microbial cells, enabling accurate species-level identification within minutes.Principle...

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Related Experiment Video

Updated: Jul 12, 2026

Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)
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Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)

Published on: December 20, 2010

Proteome-Wide Target Identification Using Reactive Metallo-Scaffolds (r-mS): A Platform for Metallodrug Discovery.

Jessica E Waters1,2, Harry Wilders3, George S Biggs3

  • 1The Biological Inorganic Chemistry Laboratory, The Francis Crick Institute, London, UK.

Angewandte Chemie (International Ed. in English)
|July 10, 2026
PubMed
Summary

Researchers developed reactive metallo-scaffolds (r-mS) to map cysteine proteins. A specific scaffold, r-mS-2, inhibited PRMT1 activity by covalently binding to cysteine 119, showcasing potential for drug discovery.

Keywords:
PRMT1bioinorganic chemistrycysteine targetingproteomicsreactive metallo scaffolds

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Area of Science:

  • Chemical biology
  • Drug discovery
  • Proteomics

Background:

  • Metal complexes offer unique scaffolds for chemical biology and drug discovery.
  • Tunable geometries and modular coordination environments are key advantages over organic molecules.

Purpose of the Study:

  • Introduce reactive metallo-scaffolds (r-mS) for mapping ligandable cysteines across the mammalian proteome.
  • Investigate how metal identity, ligand architecture, and molecular topography influence cysteine engagement.

Main Methods:

  • Utilized chemoproteomics to profile a series of r-mS in HEK293T lysate.
  • Employed intact protein LC-MS for interaction validation.
  • Performed structural modeling and docking to understand binding mechanisms.

Main Results:

  • Identified novel cysteine ligandability across the proteome.
  • r-mS-2 demonstrated potent cysteine engagement, specifically targeting cysteine 119 in PRMT1's SAM-binding domain.
  • Demonstrated functional inhibition of PRMT1 activity by r-mS-2.
  • Elucidated the molecular basis of covalent binding through structural insights.

Conclusions:

  • Reactive metallo-scaffolds (r-mS) represent a versatile platform for proteome-wide covalent ligand discovery.
  • This approach facilitates the rational development of next-generation metallodrugs.