title: Strategies for the inhibition of serine proteases.
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.
authors.affiliation: Division of Biomedicinal Chemistry, School of Pharmacy, The Queen's University of Belfast, Medical Biology Centre, Northern Ireland, United Kingdom. brian.walker@qub.ac.uk
authors.forename: B
authors.initials: B
authors.lastname: Walker
authors.forename: J F
authors.initials: JF
authors.lastname: Lynas
mesh_terms: D000818:Animals; D015195:Drug Design; D006571:Heterocyclic Compounds / Q000737:chemistry / Q000494:pharmacology; D006801:Humans; D010455:Peptides / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000494:pharmacology*
chemical_list: D006571:Heterocyclic Compounds; D010455:Peptides; D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases