| dc.contributor.author |
Kanakis, CD |
en |
| dc.contributor.author |
Tarantilis, PA |
en |
| dc.contributor.author |
Polissiou, MG |
en |
| dc.contributor.author |
Tajmir-Riahi, HA |
en |
| dc.date.accessioned |
2014-06-06T06:52:46Z |
|
| dc.date.available |
2014-06-06T06:52:46Z |
|
| dc.date.issued |
2013 |
en |
| dc.identifier.issn |
07391102 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1080/07391102.2012.742461 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/6161 |
|
| dc.subject |
Beta-lactoglobulin |
en |
| dc.subject |
Binding site |
en |
| dc.subject |
CD |
en |
| dc.subject |
Fluorescence spectroscopy |
en |
| dc.subject |
FTIR |
en |
| dc.subject |
Molecular modeling |
en |
| dc.subject |
Polyphenol |
en |
| dc.subject.other |
amino acid |
en |
| dc.subject.other |
beta lactoglobulin |
en |
| dc.subject.other |
curcumin |
en |
| dc.subject.other |
genistein |
en |
| dc.subject.other |
milk protein |
en |
| dc.subject.other |
resveratrol |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
binding affinity |
en |
| dc.subject.other |
binding site |
en |
| dc.subject.other |
bioenergy |
en |
| dc.subject.other |
circular dichroism |
en |
| dc.subject.other |
fluorescence spectroscopy |
en |
| dc.subject.other |
hydrophilicity |
en |
| dc.subject.other |
hydrophobicity |
en |
| dc.subject.other |
infrared spectroscopy |
en |
| dc.subject.other |
molecular model |
en |
| dc.subject.other |
molecular probe |
en |
| dc.subject.other |
priority journal |
en |
| dc.subject.other |
protein binding |
en |
| dc.subject.other |
protein conformation |
en |
| dc.subject.other |
protein stability |
en |
| dc.subject.other |
protein structure |
en |
| dc.subject.other |
structure analysis |
en |
| dc.title |
Probing the binding sites of resveratrol, genistein, and curcumin with milk β -lactoglobulin |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1080/07391102.2012.742461 |
en |
| heal.publicationDate |
2013 |
en |
| heal.abstract |
We determined the binding sites of curcumin (cur), resveratrol (res), and genistein (gen) with milk β-lactoglobulin (β-LG) at physiological conditions. Fourier transform infrared spectroscopy, circular dichroism, and fluorescence spectroscopic methods as well as molecular modeling were used to determine the binding of polyphenol-protein complexes. Structural analysis showed that polyphenols bind β-LG via both hydrophilic and hydrophobic contacts with overall binding constants of Kcurcumin-β-LG = 4.4 (±.4) × 104 M-1, Kresveratrol-β-LG = 4.2 (±.2) × 104 M-1, and Kgenistein-β-LG = 1.2 (±.2) × 104 M-1. The number of polyphenol molecules bound per protein (n) was 1 (cur), 1.1 (res), and 1 (gen). Molecular modeling showed the participation of several amino acid residues in polyphenol-protein complexation with the free binding energy of -12.67 (curcumin-β-LG), -12.60 (resveratrol-β-LG), and -10.68 kcal/mol (genistein-β-LG). The order of binding was cur > res > gen. Alteration of the protein conformation was observed in the presence of polyphenol with a major reduction of β-sheet and an increase in turn structure, causing a partial protein structural destabilization. β-LG might act as a carrier to transport polyphenol in vitro. © 2013 Taylor & Francis. |
en |
| heal.journalName |
Journal of Biomolecular Structure and Dynamics |
en |
| dc.identifier.issue |
12 |
en |
| dc.identifier.volume |
31 |
en |
| dc.identifier.doi |
10.1080/07391102.2012.742461 |
en |
| dc.identifier.spage |
1455 |
en |
| dc.identifier.epage |
1466 |
en |