A new class of inhibitors of human leucocyte elastase
- 22 April 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 183 (2) , 201-205
- https://doi.org/10.1016/0014-5793(85)80776-6
Abstract
Studies of the inhibition of elastases at a molecular level have resulted in the identification of protected dipeptides which are reversible and highly specific inhibitors of human leucocyte elastase (HLE). These have been further developed by increasing their hydrophilicity and potency to give a new family of elastase inhibitors, typicaly Nα -(1-adamantanesulphonyl)-Nϵ -(4-carboxybenzoyl)-L-lysyl-L-alanyl-L-valinal. These compounds are active in pharmacological models designed to detect compounds of potential therapeutic value in the treatment of emphysema.Keywords
This publication has 12 references indexed in Scilit:
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Some novel inhibitors of porcine pancreatic elastaseBioorganic Chemistry, 1979
- Drug absorption from the lungBiochemical Pharmacology, 1978
- The polymorphonuclear leukocyteInflammation Research, 1978
- Substrate specificity of the elastase and the chymotrypsin-like enzyme of the human granulocyteBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- The synthesis and analytical use of a highly sensitive and convenient substrate of elastaseBiochemical Medicine, 1974
- The Neutral Proteases of Human GranulocytesEuropean Journal of Biochemistry, 1974
- Use of peptide aldehydes to generate transition-state analogs of elastaseBiochemistry, 1973
- Substrate binding site in bovine chymotrypsin Aγ. Crystallographic study using peptide chloromethyl ketones as site-specific inhibitorsBiochemistry, 1971
- On the active site of elastase: Partial mapping by means of specific peptide substratesFEBS Letters, 1970