Unravelling the interaction mechanism between clioquinol and bovine serum albumin by multi-spectroscopic and molecular docking approaches.
Anti-Alzheimer
Bovine serum albumin
Clioquinol
Fluorescence quenching
Multi-spectral analysis
Journal
Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy
ISSN: 1873-3557
Titre abrégé: Spectrochim Acta A Mol Biomol Spectrosc
Pays: England
ID NLM: 9602533
Informations de publication
Date de publication:
05 Jun 2019
05 Jun 2019
Historique:
received:
30
09
2018
revised:
02
03
2019
accepted:
03
03
2019
pubmed:
14
3
2019
medline:
25
6
2019
entrez:
14
3
2019
Statut:
ppublish
Résumé
Clioquinol has recently been proposed for the treatment of Alzheimer's disease. It is able to diminish β-amyloid protein aggregation and to restore cognition of Alzheimer's mice. However, its therapeutic benefits for Alzheimer's disease in human remain controversy and need further confirmation. Herein, we have explored the interaction mechanism of clioquinol toward bovine serum albumin (BSA) by means of multi-spectroscopic and docking simulation approaches. Clioquinol interacts with BSA by a combined mechanism of static and dynamic processes. Application of the Hill's equation to fluorescence quenching experiment revealed that the binding constant of the BSA-clioquinol complex is extremely high at 10
Identifiants
pubmed: 30865872
pii: S1386-1425(19)30236-7
doi: 10.1016/j.saa.2019.03.004
pii:
doi:
Substances chimiques
Protein Aggregates
0
Serum Albumin, Bovine
27432CM55Q
Clioquinol
7BHQ856EJ5
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
25-34Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.