Abstract.
Serine proteases have been shown to play a multifarious role in health and disease. As a result, there has been considerable interest in the design and development of synthetic inhibitors of these enzymes. In view of their diverse roles in biological processing events, one of the great challenges in such endeavours has been the need to produce compounds with exquisite selectivity. Inhibitor design has been broadly guided by the use of either peptide- or heterocyclic-based compounds, designed to exploit the known substrate specificity characteristics of individual enzymes. This review describes the thinking and strategies employed in such efforts.
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Received 8 August 2000; received after revision 16 November 2000; accepted 17 November 2000
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Walker, B., Lynas, J. Strategies for the inhibition of serine proteases. CMLS, Cell. Mol. Life Sci. 58, 596–624 (2001). https://doi.org/10.1007/PL00000884
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DOI: https://doi.org/10.1007/PL00000884