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Rogowska, A.* ; Król-Górniak, A.* ; Railean, V.* ; Kanawati, B. ; Schmitt-Kopplin, P. ; Michalke, B. ; Sugajski, M.* ; Pomastowski, P.* ; Buszewski, B.*

Deciphering the complexes of zinc ions and hen egg white lysozyme: Instrumental analysis, molecular docking, and antimicrobial assessment.

Spectrochim. Acta A 305:123490 (2024)

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Open Access Green as soon as Postprint is submitted to ZB.

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In the research presented in this manuscript, an intricate study has been carried out on the interaction of zinc ions with the hen egg white lysozyme (HEWL) protein. Utilizing a spectroscopic technique, the alterations that arise due to the binding of Zn2+ to the HEWL were scrutinized, underscoring the paramount significance of deprotonated carboxyl and thiol groups in the process of binding. The binding phenomena were substantiated using capillary electrophoresis integrated with inductively coupled plasma mass spectrometry (CE-ICP-MS). Further spectrometric assessments (MALDI-TOF MS and FT-ICR-MS) shed light on the direct interaction of zinc ions with the functional groups of the protein. Importantly, high-resolution FT-ICR-MS techniques elucidated the capability of a single protein molecule to bind to multiple zinc ions. The empirically derived spectroscopic data received additional confirmation via a molecular docking study of the Zn2+ binding process, which highlighted a substantial affinity between the predicted 3D model of zinc-lysozyme complexes. Predominantly, the interaction between the bound entities was observed at the cysteine residues. Lastly, the conducted antimicrobial tests revealed that the zinc-lysozyme complexes manifest an inhibitory effect against bacterial (E. coli and S. aureus) and yeast (C. albicans) strains.

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords Antimicrobial Activity ; Lysozyme ; Mass Spectrometry ; Zinc Ions ; Zinc-lysozyme Complexes; Capillary-electrophoresis; Mass-spectrometry; Binding; Proteins; Beta; Stability; Divalent; Raman; Ir

ISSN (print) / ISBN 1386-1425

e-ISSN 1873-3557

Journal Spectrochimica acta, Part A

Quellenangaben Volume: 305, Article Number: 123490

Publisher Elsevier

Publishing Place Amsterdam [u.a.]

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Research Unit Analytical BioGeoChemistry (BGC)

Grants National Science Centre, Etiuda 7
European Union under the European Regional Development Fund