Bioorganic and Medicinal Chemistry Letters p. 913 - 918 (1998)
Update date:2022-08-05
Topics:
Eda, Masahiro
Ashimori, Atsuyuki
Akahoshi, Fumihiko
Yoshimura, Takuya
Inoue, Yoshihisa
Fukaya, Chikara
Nakajima, Masahide
Fukuyama, Hajime
Imada, Teruaki
Nakamura, Norifumi
Peptidyl difluoromethylene ketone derivatives were designed to take advantage of probable additional interactions with the S' subsite of human heart chymase. They showed potent inhibitory activities against human heart chymase and were more efficient than bovine chymotrypsin.
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