scholarly journals Influence of Bovine Serum Albumin-Flavonoid Interaction on the Antioxidant Activity of Dietary Flavonoids: New Evidence from Electrochemical Quantification

Molecules ◽  
2018 ◽  
Vol 24 (1) ◽  
pp. 70 ◽  
Author(s):  
Rui Geng ◽  
Lei Ma ◽  
Liangliang Liu ◽  
Yixi Xie
Keyword(s):  
Antioxidant Activity ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Masking Effect ◽  
Antioxidant Power ◽  
Spectrophotometric Methods ◽  
Ferric Reducing Antioxidant Power ◽  
New Evidence ◽  
Dietary Flavonoids

Interaction between dietary flavonoids and albumins plays an important role in the bioavailability and bioactivity of flavonoids. Therefore, the influence of this interaction on the antioxidant activity of flavonoid has attracted much interest. In this study, a ceric reducing/antioxidant capacity assay (CRAC) was employed to investigate the effects of albumin-flavonoid interaction on the antioxidant activity of seven common flavonoids. The results obtained from the CRAC assay were also compared separately with the results from the spectrophotometric methods including 2,2-diphenyl-1-picrylhydrazyl (DPPH) and ferric reducing antioxidant power (FRAP) assays. All the flavonoids show a decreasing in the antioxidant activity detected by CRAC assay, indicting a “masking effect” of bovine serum albumin (BSA)-flavonoid interaction. However, the results from DPPH and FRAP assays were conflicting, which may be attributed to the influence of solvent systems.

Antioxidant activity of bovine serum albumin binding amino acid Schiff-bases metal complexes

2007 ◽  
Vol 18 (11) ◽  
pp. 1416-1418 ◽  
Author(s):  
Rong Min Wang ◽  
Juan Juan Mao ◽  
Jing Feng Song ◽  
Cai Xia Huo ◽  
Yu Feng He
Keyword(s):  
Antioxidant Activity ◽  
Amino Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Metal Complexes ◽  
Schiff Bases ◽  
Bovine Serum ◽  
Albumin Binding ◽  
Bovine Serum Albumin Binding

Antioxidant activity of methimazole–copper(II) bioactive species and spectroscopic investigations on the mechanism of its interaction with Bovine Serum Albumin

Polyhedron ◽  
2012 ◽  
Vol 31 (1) ◽  
pp. 530-538 ◽  
Author(s):  
Nora M. Urquiza ◽  
Luciana G. Naso ◽  
Silvia G. Manca ◽  
Luis Lezama ◽  
Teófilo Rojo ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Investigations

scholarly journals Comparative Studies on the Interaction of Cochinchinenin A and Loureirin B with Bovine Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Tianming Yang ◽  
Hao Zhang ◽  
Haiyan Fu ◽  
Yuanbin She ◽  
Can Huang ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Constants ◽  
Static Quenching ◽  
Spectrophotometric Methods ◽  
Quenching Efficiency ◽  
Circular Dichroïsm ◽  
Loureirin B

This paper describes the simple, sensitive, and effective spectrophotometric methods based on ultraviolet, fluorescence and circular dichroism for revealing the interactional mechanism of Cochinchinenin A (CA) and Loureirin B (LB) with bovine serum albumin (BSA). Under simulated physiological conditions, it was demonstrated that the fluorescence quenching mechanisms between CA (or LB) and BSA as a static quenching mode, or a combined quenching (dynamic and static quenching) mode were related to concentration level of CA (or LB). The binding distance (rCA,rLB) and the quenching efficiency (KSV), especially for the binding constants value of ligands to BSA, were affected by the methoxyl group at position 4 at different temperatures. The corresponding thermodynamic parameters were also obtained and indicated that electrostatic forces play a major role in the formation of the LB-BSA complex, but probably a combined force for CA-BSA complex. Furthermore, synchronous fluorescence spectroscopy and circular dichroism spectra demonstrated that the secondary structures of BSA were changed to varying degrees by the binding of CA (or LB).

Sign in / Sign up

Export Citation Format

Share Document