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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

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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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Area of Science:

  • Biopharmaceutical Analysis
  • Analytical Chemistry
  • Mass Spectrometry

Background:

  • Peptide mapping is crucial for biopharmaceutical characterization, often relying on lengthy liquid chromatography (LC) separations.
  • Resolving critical post-translational modifications (PTMs) and isobaric peptides can be challenging with traditional LC methods.
  • Ion mobility (IM) offers an orthogonal separation mechanism based on peptide structure, complementing LC.

Purpose of the Study:

  • To evaluate the analytical capability of next-generation high-resolution ion mobility (HRIM) using structures for lossless ion manipulations (SLIM) technology for peptide mapping.
  • To assess the potential of HRIM to reduce run times and improve resolution in biopharmaceutical characterization.
  • To demonstrate the application of LC-HRIM-MS and LC-HRIM-Collision Induced Dissociation-MS (HRIM-CID-MS) for characterizing monoclonal antibodies.

Main Methods:

  • Characterization of NIST monoclonal antibody IgG1κ (NIST RM 8671) using a 20-minute LC-HRIM-MS method.
  • Employing LC-HRIM-CID-MS for enhanced sequence determination and confidence.
  • Utilizing m/z-extracted HRIM arrival time distributions for quantitative measurements of peptide modifications.

Main Results:

  • Achieved 96.5% sequence coverage for the NISTmAb.
  • HRIM-MS successfully resolved critical PTMs (oxidations, deamidations, isomerizations) that coeluted chromatographically.
  • Quantitative measurements of % modification showed good agreement with reference liquid-phase separation data.
  • Demonstrated up to 3x shorter run times compared to conventional peptide mapping methods.

Conclusions:

  • HRIM using SLIM technology significantly enhances peptide mapping workflows in biopharmaceutical characterization.
  • This technique provides superior resolution and reduces analysis time, overcoming limitations of traditional LC methods.
  • LC-HRIM-MS and LC-HRIM-CID-MS offer robust capabilities for identifying and quantifying PTMs with high confidence.