Structure-Based Drug Design of Peptide Mimetics Containing Large P3 Moieties as Inhibitors of Factor VIIa

Takuya Shiraishi,Shojiro Kadono,Masayuki Haramura,Hirofumi Kodama,Yoshiyuki Ono,Hitoshi Iikura,Tohru Esaki,Takaki Koga,Kunihiro Hattori,Yoshiaki Watanabe,Akihisa Sakamoto,Kazutaka Yoshihashi,Takehisa Kitazawa,Keiko Esaki,Masateru Ohta,Haruhiko Sato,Toshiro Kozono

LETTERS IN DRUG DESIGN & DISCOVERY（2009）

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摘要

Peptide mimetic compounds 9d and 9h showed good selectivity for FVIIa/TF over other serine proteases. Xray crystal structure analysis revealed that a large moiety at P3 interacted in a novel manner with the 170-loop and was accompanied by ligand-induced conformational change of the 170-loop. From additional optimization, we discovered compound 10b, an excellent extrinsic pathway-selective inhibitor.

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关键词

Structure-based drug design,Serine protease,FVIIa inhibitor,2 x APTT/2 x PT ratio,X-ray crystal structure,Ligand-induced conformational change

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