Monash University

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Reason: Under embargo until January 2020. After this date a copy can be supplied under Section 51(2) of the Australian Copyright Act 1968 by submitting a document delivery request through your library

Structural and Functional Studies of Plasmin Inhibitors

posted on 2019-01-15, 23:28 authored by GUOJIE WU
Human plasmin is a plasma serine protease that plays key roles in fibrinolysis, wound healing and cell migration. Accordingly, anti-fibrinolytics targeting plasmin have been widely used for treating life-threatening bleeding during surgeries or in trauma. However, current plasmin-targeting drugs are limited by poor potency or low specificity. Our researcher here characterized the functions and structures of different plasmin specific inhibitors and illustrated the inhibition mechanisms mainly via X-ray crystallography. This work revealed distinct structural features of plasmin active-site within the serine protease family, and developed highly selective plasmin inhibitors, which rationalizes structure-aided drug design and future clinical studies.


Principal supervisor

James Whisstock

Additional supervisor 1

Ruby Law

Year of Award


Department, School or Centre

Biochemistry and Molecular Biology

Campus location



Doctor of Philosophy

Degree Type



Faculty of Medicine Nursing and Health Sciences