Synthesis of novel cyclic protease inhibitors using Grubbs olefin metathesis

The unusual amino acid bishomoallylglycine was synthesized and used to form cyclic P 3P 1 tripeptide inhibitors via a Grubbs olefin metathesis method. These compounds show micro- to nanomolar inhibition of Rhizopus chinensis pepsin and represent a new class of simplified aspartic protease inhibitor...

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Veröffentlicht in:	Bioorganic & medicinal chemistry letters 1998-02, Vol.8 (4), p.357-360
Hauptverfasser:	Ripka, Amy S, Bohacek, Regine S., Rich, Daniel H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alkenes - chemistry Chemistry Exact sciences and technology Organic chemistry Peptides Preparations and properties Protease Inhibitors - chemical synthesis Protease Inhibitors - chemistry
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creator	Ripka, Amy S Bohacek, Regine S. Rich, Daniel H.
description	The unusual amino acid bishomoallylglycine was synthesized and used to form cyclic P 3P 1 tripeptide inhibitors via a Grubbs olefin metathesis method. These compounds show micro- to nanomolar inhibition of Rhizopus chinensis pepsin and represent a new class of simplified aspartic protease inhibitors lacking P′ residues. Cyclic P 3-P 1 tripeptide inhibitors were formed via a Grubbs olefin metathesis method. These compounds show micro- to nanomolar inhibition of Rhizopus chinensis pepsin.
doi_str_mv	10.1016/S0960-894X(98)00025-0
format	Article
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subjects	Alkenes - chemistry Chemistry Exact sciences and technology Organic chemistry Peptides Preparations and properties Protease Inhibitors - chemical synthesis Protease Inhibitors - chemistry
title	Synthesis of novel cyclic protease inhibitors using Grubbs olefin metathesis
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