6533b86dfe1ef96bd12c9755

RESEARCH PRODUCT

Synthesis of Tetrapeptide p‐nitrophenylanilides containing dehydroalanine and dehydrophenylalanine and their influence on cathepsin C activity

Maciej MakowskiRafał LatajkaMałgorzata PawełczakKornel NowakPaweł Kafarski

subject

Magnetic Resonance SpectroscopyStereochemistryPhenylalaninePeptideBiochemistryCathepsin CCathepsin Cdipeptidyl-peptidase Ichemistry.chemical_compoundStructural BiologyDehydroalanineDrug DiscoveryAnimalsAnilidesAmino AcidsMolecular BiologyPharmacologyCathepsinchemistry.chemical_classificationAlanineTetrapeptideChemistryOrganic ChemistryProteolytic enzymesdehydroamino acidsGeneral Medicineproteolytic enzymesAmino acidEnzymeModels ChemicalBiochemistryMolecular MedicineCattleOligopeptidesSpleen

description

Three dehydrotetrapeptides of rationally varying structure were prepared and tested as affectors of cathepsin C. These compounds appeared to be substrates of the enzyme, being equipotent with their classical counterparts. Thus, replacement of amino acid in a short peptide by corresponding dehydroamino acid does not prevent cathepsin C in recognizing dehydropeptide as its substrate. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.

yearjournalcountryeditionlanguage
2001-04-12Journal of Peptide Science
10.1002/psc.307https://onlinelibrary.wiley.com/doi/abs/10.1002/psc.307