ORBi: Beck Joséphine - Discovery of novel lipophilic inhibitors of OXA-10 enzyme (class D beta-lactamase) by screening amino analogs and homologs of citrate and isocitrate.

Reference : Discovery of novel lipophilic inhibitors of OXA-10 enzyme (class D beta-lactamase) by sc...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/23116

Title :	Discovery of novel lipophilic inhibitors of OXA-10 enzyme (class D beta-lactamase) by screening amino analogs and homologs of citrate and isocitrate.
Language :	English
Author, co-author :	Beck, Joséphine [Université Catholique de Louvain - UCL > Unité de chimie organique et médicinale > > >]
	Vercheval, Lionel [Université de Liège - ULg > > > Doct. sc. (bioch., bioch. mol.&cell., bioinf.&mod.-Bologne)]
	Bebrone, Carine [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
	Herteg-Fernea, Adriana [Université de Liège - ULG > Centre d'Ingénierie des Protéines > > >]
	Lassaux, Patricia [Université de Liège - ULg > > > Doct. sc. (bioch., bioch. mol.&cell., bioinf.&mod.-Bologne)]
	Marchand-Brynaert, Jacqueline [Université Catholique de Louvain - UCL > Unité de chimie organique et médicinale > > >]
Publication date :	1-Jul-2009
Journal title :	Bioorganic & Medicinal Chemistry Letters
Publisher :	Elsevier Science
Volume :	19
Pages :	3593-7
Audience :	International
ISSN :	0960-894X
e-ISSN :	1464-3405
City :	Oxford
Country :	United Kingdom
Abstract :	[en] Aminocitrate (and homolog) derivatives have been prepared by bis-alkylation of glycinate Schiff bases with bromoacetates (and ethyl acrylate), followed by N-acylation and esters (partial or complete) deprotection. Aminoisocitrate was similarly obtained by mono-alkylation with diethyl fumarate. Evaluation against representative beta-lactamases revealed that the free acid derivatives are modest inhibitors of class A enzymes, whilst their benzyl esters showed a good inhibition of OXA-10 (class D enzyme). A docking experiment featured hydrophobic interactions in the active site.
Funders :	Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Permalink :	http://hdl.handle.net/2268/23116
Other URL :	http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TF9-4W7B0CC-1&_user=532038&_rdoc=1&_fmt=&_orig=search&_sort=d&_docanchor=&view=c&_acct=C000026659&_version=1&_urlVersion=0&_userid=532038&md5=b0012054c5e0d79ca5d9867fd53f78fa
Mentions required by the publisher for OA :	We acknowledge Elsevier

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