The importance of Val‐157 hydrophobia interaction for papain inhibitory activity of an epoxysuccinyl amino acid derivative

FEBS Letters

Matsumoto, Keita¹  Ohishi, Hirofumi¹  Inoue, Masatoshi¹  Hanada, Kazunori²  Ishida, Toshimasa¹  Kitamura, Kunihiro²  Yamamoto, Daisuke¹ 

[1] Osaka University of Pharmaceutical Sciences, 2-10-65 Kawai, Matsubara, Osaka 580, Japan;Research Center, Taisho Pharmaceutical Co. Ltd, 1-403 Yoshino-cho, Ohmiya, Saitama 330, Japan

关键词: Papain;    Epoxysuccinyl amino acid derivative;    Inhibitory activity;    Quantitative structure-activity relationship;    Hydrophobic interaction;   

DOI  :  10.1016/0014-5793(90)80722-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Based on the crystal structure of the papain-E-64-c complex, 3-dimensional binding modes of a series of epoxysuccinyl amino acid derivatives to the papain active site have been constructed and the structure-inhibitory activity relationship has been analyzed using the accessible surface area and nonbonded energy parameters. The result indicates the importance of the hydrophobic interaction between the amino acid side chain of the inhibitor and the papain Val-157 residue for revealing the potent inhibitory activity.

【 授权许可】

Unknown