Reactions of Medicinal Gold Compounds with Cathepsin B Explored through Electrospray Mass Spectrometry Measurements.

Autor: Geri A; Department of Chemistry 'Ugo Schiff', Università di Firenze, Via della Lastruccia 3, 50019, Sesto Fiorentino, Italy., Massai L; Department of Chemistry 'Ugo Schiff', Università di Firenze, Via della Lastruccia 3, 50019, Sesto Fiorentino, Italy., Novinec M; Faculty of Chemistry and Chemical Technology, Department of Chemistry and Biochemistry, University of Ljubljana, Večna pot 113, 1000, Ljubljana, Slovenia., Turel I; Faculty of Chemistry and Chemical Technology, Department of Chemistry and Biochemistry, University of Ljubljana, Večna pot 113, 1000, Ljubljana, Slovenia., Messori L; Department of Chemistry 'Ugo Schiff', Università di Firenze, Via della Lastruccia 3, 50019, Sesto Fiorentino, Italy.
Jazyk: angličtina
Zdroj: ChemPlusChem [Chempluschem] 2024 Feb; Vol. 89 (2), pp. e202300321. Date of Electronic Publication: 2023 Nov 23.
DOI: 10.1002/cplu.202300321
Abstrakt: Medicinal gold compounds, a novel class of potential anticancer drugs, are believed to produce their pharmacological effects mainly through direct gold binding to protein targets at the level of solvent exposed cysteine (or selenocysteine) residues. We have explored therein the reactions of a panel of seven representative gold compounds with the cysteine protease cathepsin B according to an established ESI MS approach. Detailed information on the mode of protein binding of these gold compounds is gained; notably, quite distinct patterns of cathepsin B metalation have emerged from these studies. It is shown that panel gold compounds interact preferentially, often exclusively, with the free cysteine located in the active site of the enzyme.
(© 2023 The Authors. ChemPlusChem published by Wiley-VCH GmbH.)
Databáze: MEDLINE
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