362477-41-6Relevant academic research and scientific papers
New type of metalloproteinase inhibitor: Design and synthesis of new phosphonamide-based hydroxamic acids
Sawa, Masaaki,Kiyoi, Takao,Kurokawa, Kiriko,Kumihara, Hiroshi,Yamamoto, Minoru,Miyasaka, Tomohiro,Ito, Yasuko,Hirayama, Ryoichi,Inoue, Tomomi,Kirii, Yasuyuki,Nishiwaki, Eiji,Ohmoto, Hiroshi,Maeda, Yu,Ishibushi, Etsuko,Inoue, Yoshimasa,Yoshino, Kohichiro,Kondo, Hirosato
, p. 919 - 929 (2007/10/03)
A series of phosphonamide-based hydroxamate derivatives were synthesized, and the inhibitory activities were evaluated against various metalloproteinases in order to clarify its selectivity profile. Among the four diastereomeric isomers resulting from the
Encounter with unexpected collagenase-1 selective inhibitor: Switchover of inhibitor binding pocket induced by fluorine atom
Sawa, Masaaki,Kondo, Hirosato,Nishimura, Shinichiro
, p. 581 - 584 (2007/10/03)
Phosphonamide-based inhibitors having trifluoromethyl moiety showed highly selective inhibition against MMP-1. A possible mechanism of the selectivity of MMP-1 inhibitors through the switchover of the binding pocket was speculated by computational calculations. As a consequence of the unexpected selectivity, the specific interaction of CF3 group of the inhibitor and Arg214 in the S1′ pocket of MMP-1 conducted a low binding energy.
