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The importance of Val‐157 hydrophobia interaction for papain inhibitory activity of an epoxysuccinyl amino acid derivative
Author(s) -
Yamamoto Daisuke,
Matsumoto Keita,
Ohishi Hirofumi,
Ishida Toshimasa,
Inoue Masatoshi,
Kitamura Kunihiro,
Hanada Kazunori
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80722-u
Subject(s) - papain , inhibitory postsynaptic potential , chemistry , amino acid , derivative (finance) , stereochemistry , biochemistry , medicine , enzyme , financial economics , economics
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.