Combined multispectroscopic and molecular dynamics simulation investigation on the interaction between cyclosporine A and β-lactoglobulin

详细信息    查看全文

• 作者：Fatemeh S. Mohseni-Shahri^a ; ^{fmohsenishahri@gmail.com} ; Farid Moeinpour^a ; Bizhan Malaekeh-Nikouei^b ; Hooriyeh Nassirli^c
• 关键词：β-LG ; Cyclosporine A ; Fluorescence spectroscopy ; Absorption spectroscopy ; Molecular dynamics simulation
• 刊名：International Journal of Biological Macromolecules
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：95
• 期：Complete
• 页码：1-7
• 全文大小：1722 K
• 卷排序：95

文摘

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 × 105 and 0.87 × 105 M−1, 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.