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Multispectroscopic exploration and molecular docking analysis on interaction of eriocitrin with bovine serum albumin.
- Source :
-
Journal of molecular recognition : JMR [J Mol Recognit] 2019 Jul; Vol. 32 (7), pp. e2779. Date of Electronic Publication: 2019 Jan 31. - Publication Year :
- 2019
-
Abstract
- Eriocitrin is a flavanone glycoside, which exists in lemon or lime citrus fruits. It possesses antioxidant, anticancer, and anti-allergy activities. In order to investigate the pharmacokinetics and pharmacological mechanisms of eriocitrin in vivo, the interaction between eriocitrin and bovine serum albumin (BSA) was studied under the simulated physiological conditions by multispectroscopic and molecular docking methods. The results well indicated that eriocitrin and BSA formed a new eriocitrin-BSA complex because of intermolecular interactions, which was demonstrated by the results of ultraviolet-visible (UV-vis) absorption spectra. The intrinsic fluorescence of BSA was quenched by eriocitrin, and static quenching was the quenching mechanism. The number of binding sites (n) and binding constant (K <subscript>b</subscript> ) at 310 K were 1.22 and 2.84 × 10 <superscript>6</superscript>  L mol <superscript>-1</superscript> , respectively. The values of thermodynamic parameters revealed that the binding process was spontaneous, and the main forces were the hydrophobic interaction. The binding distance between eriocitrin and BSA was 3.43 nm. In addition, eriocitrin changed the conformation of BSA, which was proved by synchronous fluorescence and circular dichroism (CD) spectra. The results of site marker competitive experiments suggested that eriocitrin was more likely to be inserted into the subdomain IIA (site I), which was further certified by molecular docking studies.<br /> (© 2019 John Wiley & Sons, Ltd.)
- Subjects :
- Animals
Binding Sites
Cattle
Circular Dichroism
Flavanones chemistry
Molecular Conformation
Molecular Docking Simulation
Protein Binding
Spectrometry, Fluorescence
Spectrophotometry, Ultraviolet
Thermodynamics
Flavanones pharmacology
Serum Albumin, Bovine chemistry
Serum Albumin, Bovine metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1099-1352
- Volume :
- 32
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Journal of molecular recognition : JMR
- Publication Type :
- Academic Journal
- Accession number :
- 30701606
- Full Text :
- https://doi.org/10.1002/jmr.2779