0586459 - MBÚ 2025 RIV US eng J - Journal Article
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
R&D Projects: GA MŠMT(CZ) EF18_046/0015974
EU Projects: European Commission(XE) 823839 - EPIC-XS; European Commission(XE) 731077 - EU_FT-ICR_MS
Research Infrastructure: CIISB II - 90127
Institutional support: RVO:61388971
Keywords : mass * exchange * identification * complex * proteins * sequence
OECD category: Microbiology
Impact factor: 6.8, year: 2023 ; AIS: 1.224, rok: 2023
Method of publishing: Open access
Result website:
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.
Permanent Link: https://hdl.handle.net/11104/0354145