Synthesis of Ring II/III Fragment of Kanamycin: A New Minimum Structural Motif for Aminoglycoside Recognition

A novel protocol has been established to prepare the kanamycin ring II/III fragment, which has been validated as a minimum structural motif for the development of new aminoglycosides on the basis of its bactericidal activity even against resistant strains. Furthermore, its ability to act as a AAC-(6...

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Detalles Bibliográficos
Autores principales: Zárate, Sandra G., Bastida, Agatha, Santana, Andrés G., Revuelta, Julia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6783941/
https://www.ncbi.nlm.nih.gov/pubmed/31382490
http://dx.doi.org/10.3390/antibiotics8030109
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author Zárate, Sandra G.
Bastida, Agatha
Santana, Andrés G.
Revuelta, Julia
author_facet Zárate, Sandra G.
Bastida, Agatha
Santana, Andrés G.
Revuelta, Julia
author_sort Zárate, Sandra G.
collection PubMed
description A novel protocol has been established to prepare the kanamycin ring II/III fragment, which has been validated as a minimum structural motif for the development of new aminoglycosides on the basis of its bactericidal activity even against resistant strains. Furthermore, its ability to act as a AAC-(6′) and APH-(3′) binder, and as a poor substrate for the ravenous ANT-(4′), makes it an excellent candidate for the design of inhibitors of these aminoglycoside modifying enzymes.
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spelling pubmed-67839412019-10-16 Synthesis of Ring II/III Fragment of Kanamycin: A New Minimum Structural Motif for Aminoglycoside Recognition Zárate, Sandra G. Bastida, Agatha Santana, Andrés G. Revuelta, Julia Antibiotics (Basel) Article A novel protocol has been established to prepare the kanamycin ring II/III fragment, which has been validated as a minimum structural motif for the development of new aminoglycosides on the basis of its bactericidal activity even against resistant strains. Furthermore, its ability to act as a AAC-(6′) and APH-(3′) binder, and as a poor substrate for the ravenous ANT-(4′), makes it an excellent candidate for the design of inhibitors of these aminoglycoside modifying enzymes. MDPI 2019-08-02 /pmc/articles/PMC6783941/ /pubmed/31382490 http://dx.doi.org/10.3390/antibiotics8030109 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Zárate, Sandra G.
Bastida, Agatha
Santana, Andrés G.
Revuelta, Julia
Synthesis of Ring II/III Fragment of Kanamycin: A New Minimum Structural Motif for Aminoglycoside Recognition
title Synthesis of Ring II/III Fragment of Kanamycin: A New Minimum Structural Motif for Aminoglycoside Recognition
title_full Synthesis of Ring II/III Fragment of Kanamycin: A New Minimum Structural Motif for Aminoglycoside Recognition
title_fullStr Synthesis of Ring II/III Fragment of Kanamycin: A New Minimum Structural Motif for Aminoglycoside Recognition
title_full_unstemmed Synthesis of Ring II/III Fragment of Kanamycin: A New Minimum Structural Motif for Aminoglycoside Recognition
title_short Synthesis of Ring II/III Fragment of Kanamycin: A New Minimum Structural Motif for Aminoglycoside Recognition
title_sort synthesis of ring ii/iii fragment of kanamycin: a new minimum structural motif for aminoglycoside recognition
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6783941/
https://www.ncbi.nlm.nih.gov/pubmed/31382490
http://dx.doi.org/10.3390/antibiotics8030109
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