| dc.contributor.author |
Belatik, A |
en |
| dc.contributor.author |
Kanakis, CD |
en |
| dc.contributor.author |
Hotchandani, S |
en |
| dc.contributor.author |
Tarantilis, PA |
en |
| dc.contributor.author |
Polissiou, MG |
en |
| dc.contributor.author |
Tajmir-Riahia, HA |
en |
| dc.date.accessioned |
2014-06-06T06:52:14Z |
|
| dc.date.available |
2014-06-06T06:52:14Z |
|
| dc.date.issued |
2012 |
en |
| dc.identifier.issn |
07391102 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1080/07391102.2012.682209 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/5919 |
|
| dc.subject |
Beta-lactoglubulin |
en |
| dc.subject |
Binding site |
en |
| dc.subject |
CD |
en |
| dc.subject |
Fluorescence spectroscopy |
en |
| dc.subject |
FTIR |
en |
| dc.subject |
Modeling |
en |
| dc.subject |
Retinoid |
en |
| dc.subject.other |
amino acid |
en |
| dc.subject.other |
beta globulin |
en |
| dc.subject.other |
retinoic acid |
en |
| dc.subject.other |
retinol |
en |
| dc.subject.other |
aqueous solution |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
binding site |
en |
| dc.subject.other |
circular dichroism |
en |
| dc.subject.other |
energy |
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 |
milk |
en |
| dc.subject.other |
molecular docking |
en |
| dc.subject.other |
molecular model |
en |
| dc.subject.other |
priority journal |
en |
| dc.subject.other |
protein conformation |
en |
| dc.subject.other |
protein secondary structure |
en |
| dc.subject.other |
protein stability |
en |
| dc.subject.other |
protein structure |
en |
| dc.subject.other |
structure analysis |
en |
| dc.subject.other |
Animals |
en |
| dc.subject.other |
Binding Sites |
en |
| dc.subject.other |
Circular Dichroism |
en |
| dc.subject.other |
Hydrophobic and Hydrophilic Interactions |
en |
| dc.subject.other |
Kinetics |
en |
| dc.subject.other |
Lactoglobulins |
en |
| dc.subject.other |
Milk |
en |
| dc.subject.other |
Models, Molecular |
en |
| dc.subject.other |
Protein Binding |
en |
| dc.subject.other |
Protein Stability |
en |
| dc.subject.other |
Protein Structure, Secondary |
en |
| dc.subject.other |
Spectrometry, Fluorescence |
en |
| dc.subject.other |
Spectroscopy, Fourier Transform Infrared |
en |
| dc.subject.other |
Thermodynamics |
en |
| dc.subject.other |
Tretinoin |
en |
| dc.subject.other |
Vitamin A |
en |
| dc.title |
Locating the binding sites of retinol and retinoic acid with milk β-lactoglobulin |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1080/07391102.2012.682209 |
en |
| heal.publicationDate |
2012 |
en |
| heal.abstract |
β-lactoglobulin (β-LG) is a member of lipocalin superfamily of transporters for small hydrophobic molecules such as retinoids. We located the binding sites of retinol and retinoic acid on β-LG in aqueous solution at physiological conditions, using FTIR, CD, fluorescence spectroscopic methods, and molecular modeling. The retinoid-binding sites and the binding constants as well as the effect of retinol and retinoic acid complexation on protein stability and secondary structure were determined. Structural analysis showed that retinoids bind strongly to β-LG via both hydrophilic and hydrophobic contacts with overall binding constants of Kretinol-β-LG = 6.4 (±6) × 106M-1 and K retinoic acid-β-LG = 3.3 (±5) × 10 6M-1. The number of retinoid molecules bound per protein (n) is 1.1 (±2) for retinol and 1.5 (±3) for retinoic acid. Molecular modeling showed the participation of several amino acids in the retinoid.protein complexes with the free binding energy of -8.11 kcal/mol for retinol and -7.62 kcal/mol for retinoic acid. Protein conformation was altered with reduction of β-sheet from 59 (free protein) to 52.51% and a major increase in turn structure from 13 (free protein) to 24.22%, in the retinoid.β-LG complexes, indicating a partial protein destabilization. Copyright © 2012 Taylor & Francis. |
en |
| heal.journalName |
Journal of Biomolecular Structure and Dynamics |
en |
| dc.identifier.issue |
4 |
en |
| dc.identifier.volume |
30 |
en |
| dc.identifier.doi |
10.1080/07391102.2012.682209 |
en |
| dc.identifier.spage |
437 |
en |
| dc.identifier.epage |
447 |
en |