Synthesis of tetrapeptide p-nitrophenylanilides containing dehydroalanine and dehydrophenylalanine and their influence on cathepsin C activity.
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.
Makowski
M
M
Institute of Chemistry, University of Opole, Oleska, Poland.
Pawelczak
M
M
Latajka
R
R
Nowak
K
K
Kafarski
P
P
D000409:Alanine / Q000031:analogs & derivatives* / Q000737:chemistry*; D000596:Amino Acids / Q000737:chemistry; D000813:Anilides / Q000138:chemical synthesis* / Q000737:chemistry; D000818:Animals; D020789:Cathepsin C / Q000737:chemistry / Q000378:metabolism*; D002417:Cattle; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry*; D013154:Spleen / Q000378:metabolism
D000596:Amino Acids; D000813:Anilides; D009842:Oligopeptides; D010649:Phenylalanine; C018632:phenyldehydroalanine; C015102:dehydroalanine; D020789:Cathepsin C; D000409:Alanine