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

Biomedical Sciences (Monash Biomedicine Discovery Institute)

Additional Institution or Organisation

Biochemistry and Molecular Biology

Campus location



Doctor of Philosophy

Degree Type



Faculty of Medicine Nursing and Health Sciences