Synthesis of peptide fragments related to eglin c and examination of their inhibitory effect on human leukocyte elastase, cathepsin G and alpha-chymotrypsin.
Various kinds of peptide fragments related to eglin c were prepared by the conventional solution method and their inhibitory effects on human leukocyte elastase, cathepsin G and alpha-chymotrypsin were examined. Peptide (31-40) inhibited cathepsin G (Ki = 2.3 x 10(-4) M), peptide (41-49) potently inhibited cathepsin G and alpha-chymotrypsin (Ki = 4.2 x 10(-5) M and 2.0 x 10(-5) M, respectively), and peptide (60-63) inhibited leukocyte elastase (Ki = 1.6 x 10(-4) M), whereas, peptide (31-35) weakly inhibited both elastase and cathepsin G (Ki = 2.1 x 10(-3) M and 7.3 x 10(-4) M, respectively).
Okada
Y
Y
Faculty of Pharmaceutical Sciences, Kobe-Gakuin University, Japan.
Tsuboi
S
S
Tsuda
Y
Y
Nakabayashi
K
K
Nagamatsu
Y
Y
Yamamoto
J
J
D000595:Amino Acid Sequence; D001665:Binding Sites; D056649:Cathepsin G; D002403:Cathepsins / Q000037:antagonists & inhibitors; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D006801:Humans; D019272:Leukocyte Elastase; D007962:Leukocytes / Q000201:enzymology; D008969:Molecular Sequence Data; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D010446:Peptide Fragments / Q000138:chemical synthesis* / Q000302:isolation & purification / Q000494:pharmacology; D011480:Protease Inhibitors / Q000494:pharmacology*; D011487:Protein Conformation; D011506:Proteins / Q000494:pharmacology*; D012697:Serine Endopeptidases; D015843:Serpins
D010446:Peptide Fragments; D011480:Protease Inhibitors; D011506:Proteins; D015843:Serpins; C028656:eglin proteinase inhibitors; D002403:Cathepsins; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C534094:CTSG protein, human; D056649:Cathepsin G; D010196:Pancreatic Elastase; D019272:Leukocyte Elastase