ORBi: Zervosen Astrid - Interactions between penicillin-binding proteins (PBPs) and two novel classes of PBP inhibitors, arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-ones

Reference : Interactions between penicillin-binding proteins (PBPs) and two novel classes of PBP inh...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology Life sciences : Microbiology Human health sciences : Pharmacy, pharmacology & toxicology
	To cite this reference:	http://hdl.handle.net/2268/17338

Title :	Interactions between penicillin-binding proteins (PBPs) and two novel classes of PBP inhibitors, arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-ones
Language :	English
Author, co-author :	Zervosen, Astrid [Université de Liège - ULg > > Centre de recherches du cyclotron >]
	Lu, Wei-Ping [> > > >]
	Chen, Zhouliang [> > > >]
	White, Ronald E. [> > > >]
	Demuth, Thomas P. [> > > >]
	Frère, Jean-Marie [Université de Liège - ULg > Département des sciences de la vie > Département des sciences de la vie >]
Publication date :	Mar-2004
Journal title :	Antimicrobial Agents and Chemotherapy
Publisher :	Amer Soc Microbiology
Volume :	48
Issue/season :	3
Pages :	961-969
Audience :	International
ISSN :	0066-4804
City :	Washington
Keywords :	[en] penicillin-binding protein ; penicillin-resistance ; non-beta-lactam compound
Abstract :	[en] Several non-beta-lactam compounds were active against various gram-positive and gram-negative bacterial strains. The MICs of arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-ones were lower than those of ampicillin and cefotaxime for methicillin-resistant Staphylococcus aureus M1339 and vancomycin-resistant Enterococcus faecium EF12. Several compounds were found to inhibit the cell wall synthesis of S. aureus and the last two steps of peptidoglycan biosynthesis catalyzed by ether-treated cells of Escherichia coli or cell wall membrane preparations of Bacillus megaterium. The effects of the arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-one derivatives on E. coli PBP 3 and PBP 5, Streptococcus pneumoniae PBP 2xS (PBP 2x from a penicillin-sensitive strain) and PBP 2xR (PBP 2x from a penicillin-resistant strain), low-affinity PBP 2a of S. aureus, and the Actinomadura sp. strain R39 and Streptomyces sp. strain R61 DD-peptidases were studied. Some of the compounds exhibited inhibitory activities in the 10 to 100 muM concentration range. The inhibition of PBP 2xS by several of them appeared to be noncompetitive. The dissociation constant for the best inhibitor (K-i = 10 muM) was not influenced by the presence of the substrate.
Research units :	Centre d'Ingénierie des Protéines - CIP
Permalink :	http://hdl.handle.net/2268/17338
DOI :	10.1128/AAC.48.3.961-969.2004

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