主讲人简介：

南京大学生命科学学院教授、博士生导师，“蛋白质与多肽新药”教育部工程研究中心主任，中国生物化学与分子生物学学会“蛋白质专业委员会”委员。本科毕业于南京大学生命科学学院，博士毕业于中科院上海生命科学研究院生物化学与细胞生物学研究所，之后在美国哈佛大学医学院美国科学院院士，拉斯克奖得主Timothy Springer教授实验室从事博士后研究，2015年起在哈佛大学医学院担任讲师，2018年入选第十四批中组部“海外高层次人才”青年项目。

研究兴趣主要集中在血液和免疫系统中重要蛋白质和蛋白质复合物发挥功能的分子基础和调控机制，以及蛋白质与多肽药物设计。

代表性文章发表在Nature、Blood、 Nat Struct & Mol Biol、PNAS和 Elife等国际一流期刊上。

报告摘要：

Thrombosis manifesting within the circulation system is the leading cause for human mortality. Current treatments of thrombosis i.e. tPA have severe side effects of bleeding, limited its usage. Here, by deciphering the crystal structure of Hepassin, we discover that it harbors a high-affinity fibrin knobsbinding pocket to participate in the coagulation and fibrinolytic pathways. Hepassin binds with fibrin knobs to mediate fibrin meshwork branching. Blood clots without Hepassin exhibit feeble retraction and resistance to thrombolysis. Hepassin deficient mice possess bleedinguteri and are vulnerable to pulmonary embolism. The Fctagged protein (Thrombokine) has high thrombolytic efficacy comparable to tPA with low bleeding side effects. Thrombokine efficiently dissolves venous thrombi without viscus or brain bleeding. Furthermore, Thrombokine recanalizes blood flow promptly without promoting microvascular damage and reducing inflammation, resulting in a superior effect on the amelioration of microvascular obstruction (MVO) than tPA. Altogether, our findings illustrate the mechanism of thrombi regulated by the novel coagulation factor and provide a novel target for thrombolytic drug development.