Utilization of high-resolution mass spectrometry and data-independent analysis to track the monoclonal antibody spatial stability

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F25%3A00619327" target="_blank" >RIV/61388971:_____/25:00619327 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/25:10502969

Výsledek na webu

<a href="https://www.tandfonline.com/doi/full/10.1080/14789450.2025.2492763" target="_blank" >https://www.tandfonline.com/doi/full/10.1080/14789450.2025.2492763</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1080/14789450.2025.2492763" target="_blank" >10.1080/14789450.2025.2492763</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Utilization of high-resolution mass spectrometry and data-independent analysis to track the monoclonal antibody spatial stability

Popis výsledku v původním jazyce

Objectives: Chemical cross-linking coupled with mass spectrometry (CXMS) offers the distance constraints critical for building the structural model of protein and protein complexes and understanding dynamics of biological systems. Originally developed for protein structural models, CXMS has evolved into method for studying protein complex formation, ligand-induced conformational changes, and quantitative structural analysis using isotopically labeled cross-linkers. Methods: In this study we tested the potential of isotopically labeled MS-cleavable cross-linker to track the stability of the therapeutic monoclonal antibodies. Results: A novel isotopically labeled MS-cleavable cross-linker was synthesized, and its reactivity was successfully tested on peptide and protein standards. Further, the novel cross-linker was utilized to test the stability of selected therapeutical monoclonal antibodies, bevacizumab and trastuzumab, adopting the data-independent acquisition. Conclusion: This study reports the advantages of using combination of 13C isotopically labeled MS-cleavable cross-linkers and data-independent mass spectrometry analysis for the automated identification of cross-linked products and thus monitoring the structural rearrangement of protein structure.

Název v anglickém jazyce

Utilization of high-resolution mass spectrometry and data-independent analysis to track the monoclonal antibody spatial stability

Popis výsledku anglicky

Objectives: Chemical cross-linking coupled with mass spectrometry (CXMS) offers the distance constraints critical for building the structural model of protein and protein complexes and understanding dynamics of biological systems. Originally developed for protein structural models, CXMS has evolved into method for studying protein complex formation, ligand-induced conformational changes, and quantitative structural analysis using isotopically labeled cross-linkers. Methods: In this study we tested the potential of isotopically labeled MS-cleavable cross-linker to track the stability of the therapeutic monoclonal antibodies. Results: A novel isotopically labeled MS-cleavable cross-linker was synthesized, and its reactivity was successfully tested on peptide and protein standards. Further, the novel cross-linker was utilized to test the stability of selected therapeutical monoclonal antibodies, bevacizumab and trastuzumab, adopting the data-independent acquisition. Conclusion: This study reports the advantages of using combination of 13C isotopically labeled MS-cleavable cross-linkers and data-independent mass spectrometry analysis for the automated identification of cross-linked products and thus monitoring the structural rearrangement of protein structure.

Druh

J_SC - Článek v periodiku v databázi SCOPUS

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2025

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Expert Review of Proteomics

ISSN

1478-9450

e-ISSN

1744-8387

Svazek periodika

22

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

9

Strana od-do

199-207

Kód UT WoS článku

001471295500001

EID výsledku v databázi Scopus

2-s2.0-105003147151