title: Recent developments in inhibiting cysteine and serine proteases.
abstract: Some 20 years ago, affinity labelling was introduced to help gather information on active-site catalytic groups and the mechanisms of proteolytic enzymes. Now this knowledge is used to produce specific and selective inhibitors for these enzymes. The concept of "biospecific drug design" has stimulated progress in turning the inhibitors into therapeutically applicable agents. For instance, sales of antihypertensive drugs based on inhibitors of the angiotensin converting enzyme are expected to be over 2 billion US-$ in 1992. This partly illustrates the efforts made by many researchers to introduce strategies in potease inhibition for medicinal purposes. This review discusses some of the concepts.
authors.affiliation: Department of Biotechnology, Martin-Luther-University, Halle-Wittenberg, Saale, German Democratic Republic.
authors.forename: H U
authors.initials: HU
authors.lastname: Demuth
mesh_terms: D000345:Affinity Labels / Q000378:metabolism / Q000494:pharmacology; D000595:Amino Acid Sequence; D001665:Binding Sites; D015853:Cysteine Proteinase Inhibitors; D008969:Molecular Sequence Data; D011480:Protease Inhibitors / Q000494:pharmacology*; D015842:Serine Proteinase Inhibitors; D013329:Structure-Activity Relationship
chemical_list: D000345:Affinity Labels; D015853:Cysteine Proteinase Inhibitors; D011480:Protease Inhibitors; D015842:Serine Proteinase Inhibitors