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Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

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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.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
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Mass Spectrometric Analysis of Glycosphingolipid Antigens
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Rapid Mass Spectrometry-Based Multiattribute Method for Glycation Analysis with Integrated Afucosylation Detection

Mengjiao Xu1,2, Tao Liu1,2,3,4, Jin Xu1,2,3

  • 1State Key Laboratory of Macromolecular Drugs and Large-Scale Manufacturing, School of Pharmaceutical Sciences, Liaocheng University, Liaocheng 252059, China.

Journal of the American Society for Mass Spectrometry
|July 6, 2024
PubMed
Summary

A new mass spectrometry-based multiattribute method (MAM) enables rapid and accurate simultaneous monitoring of therapeutic antibody glycation and oxidation. This advanced platform enhances antibody product development and quality control.

Keywords:
MS-basedaccuratebroad-spectrumglycationmultiattribute methodquality controlrapidtherapeutic antibody

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Pharmaceutical Science

Background:

  • Therapeutic antibodies require rigorous quality control for attributes like glycation.
  • Current methods for glycation monitoring in multiattribute methods (MAM) are limited in speed and accuracy.
  • Glycation can affect antibody heterogeneity, function, and immunogenicity.

Purpose of the Study:

  • To develop an improved mass spectrometry-based MAM for simultaneous glycation and other quality attribute monitoring.
  • To evaluate the method's performance using therapeutic antibodies.
  • To assess glycation progression and identify oxidation under various conditions.

Main Methods:

  • Development of an improved mass spectrometry-based multiattribute method (MAM).
  • Enzymatic digestion (IdeS, Endo F2, dithiothreitol) and comparison with PNGase F.
  • Forced glycation studies in different buffer solutions.

Main Results:

  • The developed MS-based MAM accurately monitored glycation and afucosylation simultaneously.
  • Reduced sample processing time compared to routine methods, with comparable glycation results.
  • Identified 23 potential glycation sites and 4 significantly oxidized sites, with ammonium bicarbonate specifically stimulating oxidation, potentiated by glycation.

Conclusions:

  • The novel MS-based MAM offers a rapid, accurate, and broad-spectrum platform for antibody quality control.
  • This methodology enhances therapeutic antibody product development and quality assurance.
  • Understanding glycation-oxidation synergy is crucial for antibody stability and efficacy.