0586459 - MBÚ 2025 RIV US eng J - Článek v odborném periodiku
Fojtík, Lukáš - Kalaninová, Zuzana - Fiala, Jan - Halada, Petr - Chmelík, Josef - Man, Petr - Kukačka, Zdeněk - Novák, Petr
Structural Characterization of Monoclonal Antibodies and Epitope Mapping by FFAP Footprinting.
Analytical Chemistry. Roč. 96, č. 19 (2024), s. 7386-7393. ISSN 0003-2700. E-ISSN 1520-6882
Grant CEP: GA MŠMT(CZ) EF18_046/0015974
GRANT EU: European Commission(XE) 823839 - EPIC-XS; European Commission(XE) 731077 - EU_FT-ICR_MS
Výzkumná infrastruktura: CIISB II - 90127
Institucionální podpora: RVO:61388971
Klíčová slova: mass * exchange * identification * complex * proteins * sequence
Obor OECD: Microbiology
Impakt faktor: 6.8, rok: 2023 ; AIS: 1.224, rok: 2023
Způsob publikování: Open access
Web výsledku:
https://pubs.acs.org/doi/10.1021/acs.analchem.3c04161DOI: https://doi.org/10.1021/acs.analchem.3c04161

Covalent labeling in combination with mass spectrometry is a powerful approach used in structural biology to study protein structures, interactions, and dynamics. Recently, the toolbox of covalent labeling techniques has been expanded with fast fluoroalkylation of proteins (FFAP). FFAP is a novel radical labeling method that utilizes fluoroalkyl radicals generated from hypervalent Togni reagents for targeting aromatic residues. This report further demonstrates the benefits of FFAP as a new method for structural characterization of therapeutic antibodies and interaction interfaces of antigen-antibody complexes. The results obtained from human trastuzumab and its complex with human epidermal growth factor receptor 2 (HER2) correlate well with previously published structural data and demonstrate the potential of FFAP in structural biology.
Trvalý link: https://hdl.handle.net/11104/0354145