| 一种水蛭素类融合蛋白与凝血酶作用的动力学模拟 |
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| 引用本文： | 范垚,王进,杨杉,杨翔,张丽娜,华子春,朱德煦.一种水蛭素类融合蛋白与凝血酶作用的动力学模拟[J].生物化学与生物物理进展,2001,28(1):86-89. |
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| 作者姓名： | 范垚 王进 杨杉 杨翔 张丽娜 华子春 朱德煦 |
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| 作者单位： | 南京大学生命科学院生物化学系, |
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| 基金项目： | 国家自然科学基金(39970184, 79970116)、霍英东青年教师奖励基金和江苏省自然科学基金(BJ97041)资助项目. |
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| 摘 要： | 通过将凝血酶抑制剂水蛭素的C端20肽片段嫁接到血小板结合蛋白AnnexinⅤ上，可以期望获得既具有抗凝血活性，同时又具有导向性的新型工程蛋白质分子.利用计算机辅助分子设计手段模拟了该融合蛋白的分子结构，并对该融合蛋白对凝血酶的抑制作用进行了分子动力学模拟，得到了支持上述想法的结果.
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| 关 键 词： | 融合蛋白，分子动力学模拟，凝血酶 |
| 收稿时间： | 2000/1/24 0:00:00 |
| 修稿时间： | 2000年1月24日 |
Molecular Dynamics Simulation of Docking a Novel Hirudin-like Anti-coagulant Protein to Thrombin |
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| FAN Yao,WANG Jin,YANG Shan,YANG Xiang,ZHANG Li-N,HUA Zi-Chun and ZHU De-Xu.Molecular Dynamics Simulation of Docking a Novel Hirudin-like Anti-coagulant Protein to Thrombin[J].Progress In Biochemistry and Biophysics,2001,28(1):86-89. |
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| Authors: | FAN Yao WANG Jin YANG Shan YANG Xiang ZHANG Li-N HUA Zi-Chun and ZHU De-Xu |
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| Affiliation: | The State Key Laboratory of Pharmaceutical Biotechnology,Department of Biochemistry, School of Life Science, Nanjing University, Nanjing 210093, China;The State Key Laboratory of Pharmaceutical Biotechnology,Department of Biochemistry, School of Life Science, Nanjing University, Nanjing 210093, China;The State Key Laboratory of Pharmaceutical Biotechnology,Department of Biochemistry, School of Life Science, Nanjing University, Nanjing 210093, China;The State Key Laboratory of Pharmaceutical Biotechnology,Department of Biochemistry, School of Life Science, Nanjing University, Nanjing 210093, China;The State Key Laboratory of Pharmaceutical Biotechnology,Department of Biochemistry, School of Life Science, Nanjing University, Nanjing 210093, China;The State Key Laboratory of Pharmaceutical Biotechnology,Department of Biochemistry, School of Life Science, Nanjing University, Nanjing 210093, China;The State Key Laboratory of Pharmaceutical Biotechnology,Department of Biochemistry, School of Life Science, Nanjing University, Nanjing 210093, China |
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| Abstract: | Hirudin is one of the most potent anti-coagulant protein ever found, and its C-terminus is a key
domain for inhibiting thrombin. In order to enhance its specificity, a novel anti-coagulant protein was
constructed via fusing the C-terminus of hirudin to Annexin V, which was expected to sustain both anti
coagulant activity and phorspholipid affinity. The structure of the designed protein was predicted with both
molecular mechanics and dynamics. Molecular dynamics was adopted to simulate the docking interaction between
the fusion protein and thrombin. The results showed the inhibitory activity of the fusion protein to thrombin. |
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| Keywords: | fusion protein molecular dynamics simulation thrombin |
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