Design, synthesis and structure–activity relationship of a series of arginine aldehyde factor Xa inhibitors. Part 1: structures based on the (d)-Arg-Gly-Arg tripeptide sequence

Charles K Marlowe,Uma Sinha,Alice C Gunn,Robert M Scarborough

doi:10.1016/s0960-894x(99)00582-x

Design, synthesis and structure–activity relationship of a series of arginine aldehyde factor Xa inhibitors. Part 1: structures based on the (d)-Arg-Gly-Arg tripeptide sequence

Charles K Marlowe, Uma Sinha + Show 2 more

https://doi.org/10.1016/s0960-894x(99)00582-x

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Journal: Bioorganic & Medicinal Chemistry Letters	Publication Date: Jan 1, 2000
Citations: 36

Affiliation: VIR Biotechnology (United States)

#Selective Inhibitor Of Factor Xa #Factor Xa + Show 8 more

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Abstract

A series of arginine aldehyde inhibitors was designed as transition state (TS) analogues based on the known factor Xa specific substrate Cbz-d-Arg-Gly-Arg-pNA. BnSO2-(d)Arg-Gly-Arg-H (20) was found to be the most potent and selective inhibitor of factor Xa and prothrombinase activity in this series.

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