Biophysical insight into the binding mechanism of doxofylline to bovine serum albumin: An in vitro and in silico approach.
BSA, Doxofylline
Metal ions
Molecular docking
Multi-spectroscopic
Simulation
Vitamins
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:
15 Mar 2021
15 Mar 2021
Historique:
received:
20
07
2020
revised:
03
11
2020
accepted:
29
11
2020
pubmed:
19
12
2020
medline:
15
5
2021
entrez:
18
12
2020
Statut:
ppublish
Résumé
Insight into the mechanistic binding of bovine serum albumin (BSA) with doxofylline can layout pivotal enlightenment with relevance to pharmacokinetics and pharmacodynamics properties. Herein, many spectroscopic techniques and computational methods had been employed to interpret the structural and binding dynamics of BSA-doxofylline interaction. Doxofylline quenched the intrinsic fluorescence of BSA by static quenching. The stoichiometry and the binding constant of the BSA-doxofylline complex were 1:1 and in the order of 10
Identifiants
pubmed: 33338935
pii: S1386-1425(20)31275-0
doi: 10.1016/j.saa.2020.119296
pii:
doi:
Substances chimiques
Serum Albumin, Bovine
27432CM55Q
Theophylline
C137DTR5RG
doxofylline
MPM23GMO7Z
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
119296Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.