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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
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Gas Phase Separation of Modified Peptides for Activity-Based Protein Profiling.

Peter Bellotti1, Zirong Chen1,2, Charles D Warren1,2

  • 1Department of Pharmacology, Weill Cornell Medicine, Cornell University, New York, New York 10065, United States.

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|July 21, 2025
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Summary
This summary is machine-generated.

We developed timShift, a novel gas-phase method for reactive amino acid profiling. This technique enhances sensitivity and enables precise quantification of modified peptides in complex proteomes.

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Area of Science:

  • Proteomics
  • Chemical Biology
  • Analytical Chemistry

Background:

  • Profiling proteome reactivity requires identifying modified peptides amidst abundant unmodified ones.
  • Current affinity-based enrichment methods are laborious and cause analyte loss.

Purpose of the Study:

  • To introduce timShift, an in-spectrometer gas-phase approach for enhanced reactive amino acid profiling.
  • To overcome limitations of traditional affinity-based enrichment techniques.

Main Methods:

  • Exploiting modification-induced changes in peptide physical properties.
  • Utilizing a dicationic, aerodynamic, cysteine-reactive reagent to alter ion mobility.
  • Physically separating labeled peptides from unlabeled ones for targeted sequencing and quantification.

Main Results:

  • Successfully profiled over 8,200 reactive cysteine sites.
  • Demonstrated superior sensitivity compared to desthiobiotin/streptavidin enrichment, especially at low protein input.
  • Enabled activity-based protein profiling of covalent fragments and electrophiles in a 96-well plate format.

Conclusions:

  • timShift offers a highly sensitive and efficient method for reactive amino acid profiling.
  • This gas-phase approach significantly advances proteome reactivity analysis.
  • The method facilitates high-throughput activity-based protein profiling.