Journal
BIOCHIMIE
Volume 92, Issue 11, Pages 1689-1704Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2010.05.003
Keywords
Protease inhibitors; Proteases; Affinity selection; Phage display; Protein engineering
Categories
Funding
- Institut National de la Sante et de la Recherche Medicale (INSERM)
- Vaincre la Mucoviscidose
- ANR
- Region Centre
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Since its introduction by Georges Smith some 25 years ago, phage display has proved to be a powerful molecular technique for selecting proteins with desired biological properties from huge libraries. Early on, various protease inhibitor scaffolds were displayed at the surface of filamentous phages to select new inhibitors with shifted specificities and enhanced affinities towards one or more target protease(s). The past two decades have seen a number of natural protease inhibitors subjected to phage display, mostly to shift and increase their inhibitory specificity, but also to explore the molecular mechanisms by which they interact with their cognate enzymes with low or very high selectivity. This review focuses on the major uses of phage display in the field of protein protease inhibitors. The exquisite molecular mechanisms by which natural protease inhibitors prevent unwanted or excessive proteolysis in cells and tissues are also examined along with some of the general principles underlying the way phage display is applied to these molecules. (C) 2010 Elsevier Masson SAS. All rights reserved.
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