Monitoring biomolecular interaction between folic acid and bovine serum albumin.
Binding constant
Biomolecular interactions
Folic acid
Quenching mechanism of BSA
Thermodynamic fingerprint
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 Apr 2020
05 Apr 2020
Historique:
received:
05
11
2019
revised:
14
01
2020
accepted:
15
01
2020
pubmed:
26
1
2020
medline:
18
11
2020
entrez:
26
1
2020
Statut:
ppublish
Résumé
Folic acid is a bioactive food component whose deficiency can lead to a variety of health problems, while a high intake of folic acid can reduce the cytotoxicity of natural killer cells. The binding mechanism of folic acid to free bovine serum albumin (BSA) was studied using fluorescence, while the biomolecular interaction between confined-BSA and free folic acid was assessed by electrochemical methods and surface plasmon resonance. The fluorescence quenching mechanism of BSA by folic acid was found to have a static character. The thermodynamic parameters of the interaction were determined and indicated a spontaneous exothermic process with a binding constant of 8.72 × 10
Identifiants
pubmed: 31981855
pii: S1386-1425(20)30051-2
doi: 10.1016/j.saa.2020.118074
pii:
doi:
Substances chimiques
Serum Albumin, Bovine
27432CM55Q
Folic Acid
935E97BOY8
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
118074Informations de copyright
Copyright © 2020. Published by Elsevier B.V.
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.