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Related Concept Videos

Sulfur Assimilation01:20

Sulfur Assimilation

264
Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to...
264

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Tunable Heteroaromatic Sulfones Enhance in-Cell Cysteine Profiling.

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New heteroaromatic sulfone probes offer rapid and selective cysteine conjugation for in-cell proteome analysis. These reagents significantly accelerate reaction rates and improve stability, enabling efficient discovery of over 3000 reactive thiols.

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Area of Science:

  • Chemical Biology
  • Proteomics
  • Organic Chemistry

Background:

  • Cysteine conjugation is crucial for chemical biology and proteomics.
  • Existing cysteine alkylation reagents have limitations in reaction rate and stability.

Purpose of the Study:

  • To evaluate a library of heteroaromatic sulfones as novel cysteine conjugation reagents.
  • To assess the impact of structural modifications on reactivity and stability.
  • To profile these probes in cultured cells for proteome-wide thiol analysis.

Main Methods:

  • Synthesis and evaluation of diverse heteroaromatic sulfone libraries.
  • Kinetic analysis of cysteine conjugation reactions.
  • Cell-based profiling using desthiobiotin-functionalized probes.
  • Mass spectrometry-based thiol identification and quantification.

Main Results:

  • Select heteroaromatic sulfone substitutions increased reaction rates by over 3 orders of magnitude.
  • Probes achieved rapid thiol saturation in cultured cells at submillimolar concentrations.
  • Mass spectrometry identified over 3000 reactive/accessible thiols in native cellular environments.
  • Complementary cysteine detection was observed between different probe types.

Conclusions:

  • Heteroaromatic sulfones provide tunable, stable, and highly reactive scaffolds for cysteine conjugation.
  • These probes offer significant advantages over conventional reagents for in-cell proteome profiling.
  • The developed methodology enables efficient covalent ligand discovery and in-depth proteome analysis.