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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Natural and engineered kallikrein inhibitors: an emerging pharmacopoeia

Joakim E. Swedberg1 / Simon J. de Veer1 / Jonathan M. Harris1

1Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane, Queensland 4059, Australia

Corresponding author

Citation Information: Biological Chemistry. Volume 391, Issue 4, Pages 357–374, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/bc.2010.037, February 2010

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The kallikreins and kallikrein-related peptidases are serine proteases that control a plethora of developmental and homeostatic phenomena, ranging from semen liquefaction to skin desquamation and blood pressure. The diversity of roles played by kallikreins has stimulated considerable interest in these enzymes from the perspective of diagnostics and drug design. Kallikreins already have well-established credentials as targets for therapeutic intervention and there is increasing appreciation of their potential both as biomarkers and as targets for inhibitor design. Here, we explore the current status of naturally occurring kallikrein protease-inhibitor complexes and illustrate how this knowledge can interface with strategies for rational re-engineering of bioscaffolds and design of small-molecule inhibitors.

Keywords: bioscaffold; drug design; inhibitor; phage display; protease positional scanning synthetic combinatorial library; sunflower trypsin inhibitor

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