Amino Acids and Peptides. XXXVII. Synthesis of Stereoisomeric Nonapeptides Corresponding to Sequence 41-49 of Eglin c and Examination of Their Inhibitory Activity against Human Leukocyte Cathepsin G and α-Chymotrypsin

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概要

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• A nonapeptide, H-Ser-Pro-Val-Thr-Leu-Asp-Leu-Arg-Tyr-OH, corresponding to sequence 41-49 of eglin c inhibited leukocyte cathepsin G and α-chymotrypsin with K_i values of 2.2×10^<-5> and 7.2×10^<-6>M, respectively, although eglin c itself inhibited leukocyte elastase, cathepsin G and α-chymotrypsin with K_i values of 6.0×10^<-9>, 5.5×10^<-9> and 2.5×10^<-9>M, respectively. The inhibitory activity of the nonapeptide decreased following incubation with cathepsin G due to the cleavage of the Leu^<45>-Asp^<46> peptide bond. Therefore, Leu^<45> and/or Asp^<46> were replaced with D-amino acids and the inhibitory activities of the resultant nonapeptides were examined. Their inhibitory activities against cathepsin G and α-chymotrypsin were much weaker than those of the all-L-type nonapeptide, suggesting that the amino acids at the active site, Leu^<45> and Asp^<46> are required to be in the L-configuration for potent activity.

• 社団法人日本薬学会の論文
• 1994-07-15

著者

• 岡田 芳男

  Faculty of Pharmaceutical Sciences Kobe-Gakuin University

• 永松 陽子

  Faculty Of Nutrition Kobe-gakuin University

• 藤井 亜弓

  Faculty of Pharmaceutical Sciences Kobe-Gakuin University

• 坪井 諭志

  Faculty of Pharmaceutical Sciences Kobe-Gakuin University

• 浅田 圭一

  Faculty of Pharmaceutical Sciences Kobe-Gakuin University

• 山本 順一郎

  Faculty of Nutrition, Kobe-Gakuin University

• 岡田 芳男

  神戸学院大学 薬学部

• 山本 順一郎

  Faculty Of Nutrition Kobe-gakuin University

• Asada K

  Faculty Of Pharmaceutical Sciences Kobe-gakuin University

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