208591-36-0Relevant academic research and scientific papers
Peptidyl human heart chymase inhibitors. 2. Discovery of highly selective difluoromethylene ketone derivatives with glu at P3 site
Eda, Masahiro,Ashimori, Atsuyuki,Akahoshi, Fumihiko,Yoshimura, Takuya,Inoue, Yoshihisa,Fukaya, Chikara,Nakajima, Masahide,Fukuyama, Hajime,Imada, Teruaki,Nakamura, Norifumi
, p. 919 - 924 (1998)
Appropriate structural modification of the difluoromethylene ketone derivatives at both P3 and P' positions led us to the discovery of peptidyl human heart chymase inhibitor 12h which shows potent activity with Ki = 6 nM and high selectivity against closely related serine protease bovine a- chymotrypsin (chymotrypsin Ki = >100 μM). Using the compound 12b, a docking study with human heart chymase was carded out to presume probable interactions.
