Direct-MS analysis of antibody-antigen complexes

Shay Vimer, Gili Ben-Nissan, Michael Marty, Sarel J. Fleishman, Michal Sharon

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

In recent decades, antibodies (Abs) have attracted the attention of academia and the biopharmaceutical industry due to their therapeutic properties and versatility in binding a vast spectrum of antigens. Different engineering strategies have been developed for optimizing Ab specificity, efficacy, affinity, stability and production, enabling systematic screening and analysis procedures for selecting lead candidates. This quality assessment is critical but usually demands time-consuming and labor-intensive purification procedures. Here, we harnessed the direct-mass spectrometry (direct-MS) approach, in which the analysis is carried out directly from the crude growth media, for the rapid, structural characterization of designed Abs. We demonstrate that properties such as stability, specificity and interactions with antigens can be defined, without the need for prior purification.

Original languageEnglish (US)
Article number2000300
JournalProteomics
Volume21
Issue number21-22
DOIs
StatePublished - Nov 2021

Keywords

  • antibody antigen interactions
  • antibody deign
  • native mass spectrometry
  • protein stability

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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