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ID: ALA1156606

Journal: Bioorg Med Chem Lett

Title: Factor VIIa inhibitors: target hopping in the serine protease family using X-ray structure determination.

Authors: Shiraishi T, Kadono S, Haramura M, Kodama H, Ono Y, Iikura H, Esaki T, Koga T, Hattori K, Watanabe Y, Sakamoto A, Yoshihashi K, Kitazawa T, Esaki K, Ohta M, Sato H, Kozono T.

Abstract: Selective factor VIIa-tissue factor complex (FVIIa/TF) inhibition is regarded as a promising target for developing new anticoagulant drugs. Compound 1 was discovered from focused screening of serine protease-directed compounds from our internal collection. Using parallel synthesis supported by structure-based drug design, we identified peptidemimetic FVIIa/TF inhibitors (compounds 4-11) containing L-Gln or L-Met as the P2 moiety. However, these compounds lacked the selectivity of other serine proteases in the coagulation cascade, especially thrombin. Further optimization of these compounds was carried out with a focus on the P4 moiety. Among the optimized compounds, 12b-f showed improved selectivity.

CiteXplore: 18674905

DOI: 10.1016/j.bmcl.2008.07.044