作者: Behafarid Ghalandari , Adeleh Divsalar , Ali Akbar Saboury , Thomas Haertlé , Kazem Parivar
DOI: 10.1016/J.SAA.2013.09.126
关键词: Gibbs free energy 、 Docking (molecular) 、 Circular dichroism 、 Chemistry 、 Hydrophobic effect 、 Binding site 、 Protein secondary structure 、 Computational chemistry 、 Fluorescence 、 Förster resonance energy transfer 、 Instrumentation (computer programming) 、 Analytical chemistry 、 Spectroscopy 、 Atomic and Molecular Physics, and Optics
摘要: Abstract The possibility of using a small cheap dairy protein, β-lactoglobulin (β-LG), as carrier for oxali–palladium drug delivery was studied. Their binding in an aqueous solution at two temperatures 25 and 37 °C investigated spectroscopic techniques combination with molecular docking study. Fluorescence intensity changes showed combined static dynamic quenching during β-LG binding, the mode being predominant mechanism. thermodynamic parameters were determined by analyzing results those van’t Hoff equation. According to obtained constants are 3.3 × 10 9 M −1 18.4 × 10 6 respectively. resonance energy transfer (FRET) that experimental coherent. An absence change secondary structure confirmed CD results. Molecular agreed fully since fluorescence studies also revealed presence sites negative value Gibbs free β-LG. Furthermore, suggest hydrophobic effect plays critical role formation complex This agreement between implies may be suitable method predicting confirming results, shown this Hence, spectroscopy methods is effective innovative approach studies, particularly pharmacophores.