The effect of chrysin binding on the conformational dynamics and unfolding pathway of human serum albumin.
Chrysin
Conformational dynamics
Human serum albumin
Red edge excitation shift
Urea-induced unfolding
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:
24 Apr 2024
24 Apr 2024
Historique:
received:
29
11
2023
revised:
20
03
2024
accepted:
22
04
2024
medline:
28
4
2024
pubmed:
28
4
2024
entrez:
27
4
2024
Statut:
aheadofprint
Résumé
Studies on the interactions between ligands and proteins provide insights into how a possible medication alters the structures and activities of the target or carrier proteins. The natural flavonoid aglycone Chrysin (CHR) has demonstrated anti-inflammatory, antioxidant, antiapoptotic, neuroprotective, and antineoplastic effects, both in vitro and in vivo. In this work, we investigated the impact of CHR binding on the as-yet-unexplored conformation, dynamics, and unfolding mechanism of human serum albumin (HSA). We determined CHR binding to HSA domain-II with the association constant (K
Identifiants
pubmed: 38676982
pii: S1386-1425(24)00498-0
doi: 10.1016/j.saa.2024.124332
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
124332Informations de copyright
Copyright © 2024 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.