کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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5512369 | 1540223 | 2017 | 7 صفحه PDF | دانلود رایگان |
β-Lactoglobulin (β-LG), the major whey protein in milks of many mammals, has a high affinity for a wide range of compounds. Cyclosporine A (CsA), is an immunosuppressant drug mainly prescribe in organ transplantation to prevent rejection. In this study, the interaction of CsA with β-LG was investigated using various spectroscopic techniques (UV-visible and fluorescence) in an aqueous medium at two temperatures of 298 and 310 K in combination with a molecular dynamics simulation study. The titration results indicated that CsA quenched the fluorescence intensity of β-LG through a static mechanism. The binding constants for the binding of CsA to β-LG at two different temperatures 298 and 310 K were obtained 1.12 Ã 105 and 0.87 Ã 105 Mâ1, respectively. Thermodynamic data indicated that the hydrophobic interactions and hydrogen bonds dominate in the binding site. Results of fluorescence resonance energy transfer (FRET) measurements suggest that resonance energy transfer occurs between β-LG and CsA. Moreover, MD simulation results implied that CsA can interact with β-LG, without affecting the secondary structure of β-LG. Experimental and MD simulations data reciprocally supported each other.
Journal: International Journal of Biological Macromolecules - Volume 95, February 2017, Pages 1-7