Simulation of the inhibitory cystatin surface by a synthetic peptide.
An inhibitory dodecameric peptide was designed which tentatively mimics the inhibitory site of cystatin C-like structures. Succinylated and mansylated derivatives were also synthesised and assayed for their inhibiting properties towards papain and rat cathepsins B, H and L. All peptides preferentially inhibit cathepsin L and papain as their naturally occurring inhibitor model. A significant increase in inhibition was obtained after mansylation of the crude peptide with Ki values in the micromolar or 0.1 micromolar range. The use and interest of such peptide inhibitors are discussed.
Moreau
T
T
Laboratoire de Biochimie URA CNRS 1334, Faculté de Médecine, Université François Rabelais, Tours, France.
Hoebeke
J
J
Lalamanach
G
G
Hattab
M
M
Gauthier
F
F
D000595:Amino Acid Sequence; D000818:Animals; D002403:Cathepsins / Q000037:antagonists & inhibitors; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D015891:Cystatins / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D010206:Papain / Q000037:antagonists & inhibitors; D010455:Peptides / Q000494:pharmacology*; D051381:Rats; D013056:Spectrophotometry, Ultraviolet
D015891:Cystatins; D010455:Peptides; D002403:Cathepsins; D010206:Papain