Amino Acids and Peptides. XX. : Inhibition of Papain by Succinyl-Gln-Val-Val-Ala-p-Nitroanilide, a Common Sequence of Endogenous Thiol Proteinase Inhibitors

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概要

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• Thiol proteinase inhibitors isolated from various tissues have a fairly conservative common amino acid sequence, Gln-Val-Val-Ala-Gly. We synthesized various kinds of Gln-Val-Val-Ala-Gly derivatives by the solution method. Z-Gln-Val-Val-Ala-Ala-pNA, Z-Gln-Val-Val-Ala-pNA and Z-Gln-Val-Val-pNA weakly inhibited the amidolytic activity of papain toward Bz-Arg-βNA and exhibited a stronger protective activity than corresponding Z-peptide methyl ester against thiol proteinase inhibitor (such as T-kininogen)-induced inhibition of papain.Suc-Gln-Val-Val-Ala-Ala-pNA exhibited more potent inhibitory activity toward papain than Z-Gln-Val-Val-Ala-Ala-pNA, but it did not show any protective effect. The circular dichroism spectra of the pNA derivatives and papain suggested that the pNA moiety of the peptide participated in binding with some part of the enzyme other than the catalytic site.

• 公益社団法人日本薬学会の論文
• 1988-06-25

著者

• 坪井 諭志

  Faculty of Pharmaceutical Sciences Kobe-Gakuin University

• 中林 和則

  Faculty of Pharmaceutical Sciences, Kobe-Gakuin University

• 岡本 博

  Faculty Of Pharmaceutical Sciences Kobe-gakuin University

• 伊藤 徳夫

  Department of Pharmacology, Faculty of Pharmaceutical Sciences

• 伊藤 徳夫

  Department Of Pharmacology Faculty Of Pharmaceutical Sciences

• 岡田 芳男

  神戸学院大学 薬学部

• 岡田 芳男

  Department of Dermatology

• 手納 直規

  Faculty Of Pharmaceutical Sciences Kobe-gakuin University

• 西 則雄

  Faculty Of Science Hokkaido University

• 手納 直規

  Departments of Medicinal Chemistry

• 坪井 諭志

  Departments of Medicinal Chemistry

• 中林 和則

  Departments of Medicinal Chemistry

• 伊藤 徳夫

  Pharmacology

• 岡本 博

  Pharmacology

• 中林 和則

  Faculty Of Pharmaceutical Sciences Kobe-gakuin University

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