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Synthesis of a trihexacontapeptide corresponding to the sequence 8–70 of eglin c and studies on the relationship between the structure and the inhibitory activity against human leukocyte elastase, cathepsin G and α‐chymotrypsin
Author(s) -
Okada Yoshio,
Tsuboi Satoshi,
Tsuda Yuko,
Nagamatsu Yoko,
Yamamoto Junichiro
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)80461-q
Subject(s) - chymotrypsin , elastase , cathepsin g , cathepsin , chemistry , cathepsin l1 , pancreatic elastase , inhibitory postsynaptic potential , stereochemistry , enzyme , peptide , biochemistry , cathepsin b , microbiology and biotechnology , trypsin , biology , endocrinology
A trihexacontapeptide corresponding to the sequence 8–70 of eglin c and its related peptides were synthesized by the conventional solution method and their inhibitory activity against human leukocyte elastase, cathepsin G and α‐chymotrypsin was examined. Although synthetic eglin c (41–49) inhibited cathepsin G and α‐chymotrypsin ( K i = 4.0 × 10 −5 M and 2.0 × 10 −5 M, respectively) but not leukocyte elastase, the synthetic trihexaconta‐peptide potently inhibited cathepsin G, α‐chymotrypsin and leukocyte elastase ( K i = 1.8 × 10 −9 M, 1.4 × 10 −9 M and 2.2 × 10 −9 M, respectively). The relationship between the stucture of eglin c and the inhibitory activity against the above enzymes is also described.