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A Simple Structural-Based Approach to Prevent Aminoglycoside Inactivation by Bacterial Defense Proteins. Conformational Restriction Provides Effective Protection against Neomycin-B Nucleotidylation by ANT4

descriptionPublicationkeyboard_double_arrow_right Article 17 May 2005 Spain English Publisher:American Chemical Society (ACS)Journal:Journal of the American Chemical Society, volume 127, pages 8,278-8,279 (issn: 0002-7863, eissn: 1520-5126,

Authors: Asensio, Juan Luis; Hidalgo, Ana; Bastida, Agatha; Torrado, Mario; Corzana, Francisco; Chiara, José Luis; García-Junceda, Eduardo; +2 Authors

doi: 10.1021/ja051722z

pmid: 15941249

handle: 10261/30951

A Simple Structural-Based Approach to Prevent Aminoglycoside Inactivation by Bacterial Defense Proteins. Conformational Restriction Provides Effective Protection against Neomycin-B Nucleotidylation by ANT4

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Abstract

Herein, we describe how the conformational differences exhibited by aminoglycosides in the binding pockets of the ribosome and those enzymes involved in bacterial resistance can be exploited in the design of new antibiotic derivatives with improved activity in resistant strains. The simple modification shown in the figure, leading to the conformationally restricted 5, provides an effective protection against aminoglycoside inactivation by Staphylococcus aureus ANT4, both in vivo and in vitro.

Country

Spain

Related Organizations

Spanish National Research Council
Spain
Instituto de Química Orgánica General
Spain

Keywords

Staphylococcus aureus, Microbial Sensitivity Tests, Nucleotidyltransferases, Anti-Bacterial Agents, Structure-Activity Relationship, Aminoglycosides, Carbohydrate Conformation, Escherichia coli, Mitochondrial ADP, ATP Translocases, Nuclear Magnetic Resonance, Biomolecular, Framycetin

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