Metallodrug-protein interaction probed by synchrotron terahertz and neutron scattering spectroscopy.
Journal
Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626
Informations de publication
Date de publication:
03 08 2021
03 08 2021
Historique:
received:
31
03
2021
revised:
20
05
2021
accepted:
08
06
2021
pubmed:
3
7
2021
medline:
12
8
2021
entrez:
2
7
2021
Statut:
ppublish
Résumé
This experimental work applied coherent synchrotron-radiation terahertz spectroscopy and inelastic neutron scattering to address two processes directly associated with the mode of action of metal-based anticancer agents that can severely undermine chemotherapeutic treatment: drug binding to human serum albumin, occurring during intravenous drug transport, and intracellular coordination to thiol-containing biomolecules (such as metallothioneins) associated with acquired drug resistance. Cisplatin and two dinuclear platinum (Pt)- and palladium (Pd)-polyamine agents developed by this research group, which have yielded promising results toward some types of human cancers, were investigated. Complementary synchrotron-radiation-terahertz and inelastic neutron scattering data revealed protein metalation, through S- and N-donor ligands from cysteine, methionine, and histidine residues. A clear impact of the Pt and Pd agents was evidenced, drug binding to albumin and metallothionein having been responsible for significant changes in the overall protein conformation, as well as for an increased flexibility and possible aggregation.
Identifiants
pubmed: 34214537
pii: S0006-3495(21)00499-9
doi: 10.1016/j.bpj.2021.06.012
pmc: PMC8390959
pii:
doi:
Substances chimiques
Antineoplastic Agents
0
Cisplatin
Q20Q21Q62J
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3070-3078Informations de copyright
Copyright © 2021 Biophysical Society. Published by Elsevier Inc. All rights reserved.
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