Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods.
fluorescence quenching
hydrophobic interaction
molecular docking
secondary structure content
thermodynamic parameters
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
22 Aug 2021
22 Aug 2021
Historique:
received:
17
07
2021
revised:
19
08
2021
accepted:
19
08
2021
entrez:
27
8
2021
pubmed:
28
8
2021
medline:
18
9
2021
Statut:
epublish
Résumé
Effect of temperature and pH on the interaction of curcumin with β-casein was explored by fluorescence spectroscopy, ultraviolet-visible spectroscopy and molecular dynamics simulation. The spectroscopic results showed that curcumin could bind to β-casein to form a complex which was driven mainly by electrostatic interaction. The intrinsic fluorescence of β-casein was quenched by curcumin through static quenching mechanism. The binding constants of curcumin to β-casein were 6.48 × 10
Identifiants
pubmed: 34443680
pii: molecules26165092
doi: 10.3390/molecules26165092
pmc: PMC8398086
pii:
doi:
Substances chimiques
Caseins
0
Curcumin
IT942ZTH98
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Fundamental Research Funds for the Central Universities
ID : XDJK2019B056
Organisme : Venture & Innovation Support Program for Chongqing Overseas Returnees
ID : cx2018098
Organisme : Chongqing Municipal Training Program of Innovation and Entrepreneurship for Undergraduates
ID : S202010635165
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