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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.
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Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and signal-to-noise ratio for the analyte. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.
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Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
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MALDI-TOF Mass Spectrometry01:19

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Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.
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An HS-MRM Assay for the Quantification of Host-cell Proteins in Protein Biopharmaceuticals by Liquid Chromatography Ion Mobility QTOF Mass Spectrometry
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High-Throughput and Format-Agnostic Mispairing Assay for Multispecific Antibodies Using Intact Mass Spectrometry.

Tanja Ziegengeist1, Jennifer Orth1, Katja Kroll1

  • 1Large Molecules Research Platform, Sanofi-Aventis Deutschland GmbH, Frankfurt 65926, Germany.

Analytical Chemistry
|June 27, 2023
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Summary

A new high-throughput mass spectrometry workflow automates the analysis of multispecific antibodies, improving the detection of mispaired chains. This innovation accelerates complex protein engineering and discovery campaigns for therapeutic antibodies.

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Area of Science:

  • Biopharmaceutical development
  • Protein engineering
  • Analytical chemistry

Background:

  • Multispecific antibodies offer therapeutic advantages by engaging multiple targets.
  • Ensuring correct light and heavy chain assembly is critical for antibody function.
  • Current analytical methods for mispairing analysis lack high-throughput capabilities.

Purpose of the Study:

  • To develop a high-throughput workflow for analyzing mispaired multispecific antibodies.
  • To automate data analysis for faster identification of mispaired species.
  • To enable efficient screening of complex antibody formats.

Main Methods:

  • Development of a high-throughput mispairing workflow using intact mass spectrometry.
  • Automated data analysis, peak detection, and relative quantification with Genedata Expressionist.
  • Application to engineering a trispecific antibody and analyzing diverse multispecific formats.

Main Results:

  • The workflow successfully detects mispaired species in approximately 1000 multispecific antibodies within three weeks.
  • The system automatically annotates product-related impurities beyond mispairing.
  • The assay demonstrated format-agnostic capabilities across various multispecific antibody formats.

Conclusions:

  • The automated intact mass spectrometry workflow provides a universal, high-throughput tool for detecting and annotating peaks in multispecific antibodies.
  • This enables efficient support for complex antibody discovery campaigns.
  • The method accelerates biopharmaceutical development by streamlining analytical processes.