a Interdisciplinary Biotechnology Unit , Aligarh Muslim University , Aligarh 202002 , India.
b Department of Biochemistry, Faculty of Sciences , University of Tabuk , Tabuk 71491 , Kingdom of Saudi Arabia.
J Biomol Struct Dyn. 2019 Apr;37(6):1390-1401. doi: 10.1080/07391102.2018.1461686. Epub 2018 Apr 25.
Alpha1-acid glycoprotein (AAG) is a major acute phase protein of human plasma. Binding of clofazimine to AAG is investigated using optical spectroscopy and molecular docking tools. We found significant quenching of intrinsic fluorescence of AAG upon the binding of clofazimine, binding mode is static with binding constant of 3.52 × 10at 298 K. The Gibbs free energy change is found to be negative for the interaction of clofazimine with AAG indicating spontaneity of the binding process. Binding of clofazimine induced ordered structure in protein and lead to molecular compaction. Molecular docking results indicate the binding site is located in the central beta barrel, hydrogen bonding and hydrophobic interactions are main bonding forces between AAG-clofazimine.
α1-酸性糖蛋白（AAG）是人类血浆中的主要急性期蛋白。使用光谱学和分子对接工具研究了氯法齐明与 AAG 的结合。我们发现，氯法齐明与 AAG 结合后，AAG 的固有荧光显著猝灭，结合模式为静态，结合常数为 3.52×10^-4M^-1，在 298 K 时。结合自由能变化为负，表明氯法齐明与 AAG 的相互作用是自发的。氯法齐明的结合诱导蛋白质有序结构并导致分子紧缩。分子对接结果表明，结合位点位于中央β桶中，氢键和疏水相互作用是 AAG-氯法齐明之间的主要结合力。
