Resveratrol Binding to Fibrinogen and its Biological Implication
Resveratrol Binding to Fibrinogen and its Biological Implication
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白藜芦醇与纤维蛋白原的结合及其生物学意义
DOI：
10.1007/s11483-011-9240-1
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发表时间：
2012-03-01
期刊：
影响因子：
3
通讯作者：
Huang, Jun-Yi
中科院分区：
文献类型：
--
作者：
Zhang, Juan;Dai, Xiao-Feng;Huang, Jun-Yi
鉴于纤维蛋白原和白藜芦醇在血小板聚集和血栓形成中的重要作用，研究了二者之间的相互作用，并进一步阐明了其生物学意义。纤维蛋白原与白藜芦醇可形成1：1的复合物，其结合常数为1.11 × 10（4）M-1。结合是自发的，纤维蛋白原/白藜芦醇复合物的形成是一个外显反应。电子相互作用和氢键作用起主要作用，非辐射能量从纤维蛋白原转移到白藜芦醇。动力学研究表明，白藜芦醇与纤维蛋白原的结合随时间的延长呈沿着线性关系。白藜芦醇的添加改变了纤维蛋白原的构象，包括其二级结构，导致酪蛋白残基周围的极性增加，蛋白质中的α螺旋结构减少。此外，纤维蛋白原明显增加白藜芦醇的稳定性。这将使人们对白藜芦醇作为一种功能因子有更深入的了解。
In light of important implication of fibrinogen and resveratrol in the platelet aggregation and thrombus formation, the interaction between them was studied, and its biological implication was further explained. Fibrinogen could interact with resveratrol to form 1:1 complex with the binding constant of 1.11 x 10(4) M-1. The binding was spontaneous and fibrinogen/resveratrol complex formation was an exothermal reaction. Electronic interaction and hydrogen bonding played key roles and non-radiation energy transferred from fibrinogen to resveratrol in the binding process. Kinetic study indicated that resveratrol linearly combined to fibrinogen along with the prolonged time. The addition of resveratrol changed fibrinogen conformation including its second structure resulting in increase of polarity around tyrophore residue and decrease of alpha-helical structure in the protein. Additionally, fibrinogen obviously increased resveratrol stability. It would give a deeper insight into resveratrol as a kind of functional factor.