主講人簡介：

南京大學生命科學EON4教授👨‍👧、博士生導師🙆🏼，“蛋白質與多肽新藥”教育部工程研究中心主任🖕🏼，中國生物化學與分子生物學學會“蛋白質專業委員會”委員🆒。本科畢業於南京大學生命科學EON4，博士畢業於中科院上海生命科學研究院生物化學與細胞生物學研究所👳🏿，之後在美國哈佛大學醫EON4美國科EON4院士，拉斯克獎得主Timothy Springer教授實驗室從事博士後研究🛤，2015年起在哈佛大學醫EON4擔任講師，2018年入選第十四批中組部“海外高層次人才”青年項目。

研究興趣主要集中在血液和免疫系統中重要蛋白質和蛋白質復合物發揮功能的分子基礎和調控機製🏬，以及蛋白質與多肽藥物設計🤧。

代表性文章發表在Nature𓀄、Blood👩🏼‍🚀、 Nat Struct & Mol Biol、PNAS和 Elife等國際一流期刊上。

報告摘要：

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.