Entropy-driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching.
albumin
ascorbic acid
ascorbyl palmitate
entropy
fluorescence quenching
hydrophobic effect
octyl gallate
Journal
Journal of molecular recognition : JMR
ISSN: 1099-1352
Titre abrégé: J Mol Recognit
Pays: England
ID NLM: 9004580
Informations de publication
Date de publication:
07 2020
07 2020
Historique:
received:
18
11
2019
revised:
25
01
2020
accepted:
10
02
2020
pubmed:
3
3
2020
medline:
10
8
2021
entrez:
3
3
2020
Statut:
ppublish
Résumé
Fluorescence quenching is widely used to obtain association constants between proteins and ligands. This methodology is based on assumption that ground-state complex between protein and ligand is responsible for quenching. Here, we call the attention about the risk of using the temperature criterion for decision of applying or not fluorescence quenching data to measure association constants. We demonstrated that hydrophobic effect can be the major force involved in the interaction and, as such, superposes the well-established rationalization that host/guest complexation is weakened at higher temperatures due to loss of translational and rotational degrees of freedom. To do so, the complexation of bovine serum albumin with octyl gallate was studied by steady-state, time-resolved fluorescence spectroscopy and isothermal titration calorimetry. The results clearly demonstrated the complexation, even though the Stern-Volmer constant increased at higher temperatures (1.6 × 10
Substances chimiques
Albumins
0
octyl gallate
079IIA2811
Gallic Acid
632XD903SP
Ascorbic Acid
PQ6CK8PD0R
6-O-palmitoylascorbic acid
QN83US2B0N
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2840Informations de copyright
© 2020 John Wiley & Sons Ltd.
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