Browsing by Autor "Julia Revuelta"

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Chondroitin Sulfate-Degrading Enzymes as Tools for the Development of New Pharmaceuticals
(Multidisciplinary Digital Publishing Institute, 2019) Raúl Benito-Arenas; Sandra G. Zárate; Julia Revuelta; Ágatha Bastida
Chondroitin sulfates are linear anionic sulfated polysaccharides found in biological tissues, mainly within the extracellular matrix, which are degraded and altered by specific lyases depending on specific time points. These polysaccharides have recently acquired relevance in the pharmaceutical industry due to their interesting therapeutic applications. As a consequence, chondroitin sulfate (CS) lyases have been widely investigated as tools for the development of new pharmaceuticals based on these polysaccharides. This review focuses on the major breakthrough represented by chondroitin sulfate-degrading enzymes and their structures and mechanisms of function in addition to their major applications.
Overcoming Aminoglycoside Enzymatic Resistance: Design of Novel Antibiotics and Inhibitors
(Multidisciplinary Digital Publishing Institute, 2018) Sandra G. Zárate; M. De la Cruz Claure; Raúl Benito-Arenas; Julia Revuelta; Andrés G. Santana; Ágatha Bastida
Resistance to aminoglycoside antibiotics has had a profound impact on clinical practice. Despite their powerful bactericidal activity, aminoglycosides were one of the first groups of antibiotics to meet the challenge of resistance. The most prevalent source of clinically relevant resistance against these therapeutics is conferred by the enzymatic modification of the antibiotic. Therefore, a deeper knowledge of the aminoglycoside-modifying enzymes and their interactions with the antibiotics and solvent is of paramount importance in order to facilitate the design of more effective and potent inhibitors and/or novel semisynthetic aminoglycosides that are not susceptible to modifying enzymes.
Synthesis of Ring II/III Fragment of Kanamycin: A New Minimum Structural Motif for Aminoglycoside Recognition
(Multidisciplinary Digital Publishing Institute, 2019) Sandra G. Zárate; Ágatha Bastida; Andrés G. Santana; Julia Revuelta
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.