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      Preparation and Microbiological Evaluation of Amphiphilic Kanamycin-Lipoamino Acid Ion-Pairs

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          Abstract

          Amphiphilic ion-pairs of kanamycin (KAN) were prepared by evaporation of a water-ethanol co-solution of KAN base and a lipoamino acid bearing a 12-carbon atoms alkyl side chain (LAA12), at different molar ratios. Infrared spectroscopy confirmed the structure of ion-pairs, while differential scanning calorimetry (DSC) and powder X-ray diffractometry (PXRD) studies supported the formation of new saline species with a different crystalline structure than the starting components. The solubility pattern shown in a range of both aqueous and organic solvents confirmed that the ion-pairs possess an amphiphilic character. The LAA12 counter-ion showed not to improve the antibacterial activity of KAN, suggesting that such chemical strategy is not able to favor the penetration of this drug inside the bacteria cells. Nevertheless, a slight improving, i.e., a one-fold dilution, was observed in E. coli. The present study can also serve as the basis for a further evaluation of LAA ion-pairing of antibiotics, as a means to improve the loading of hydrophilic drugs into lipid-based nanocarriers.

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          The porin and the permeating antibiotic: a selective diffusion barrier in Gram-negative bacteria.

          Gram-negative bacteria are responsible for a large proportion of antibiotic-resistant bacterial diseases. These bacteria have a complex cell envelope that comprises an outer membrane and an inner membrane that delimit the periplasm. The outer membrane contains various protein channels, called porins, which are involved in the influx of various compounds, including several classes of antibiotics. Bacterial adaptation to reduce influx through porins is an increasing problem worldwide that contributes, together with efflux systems, to the emergence and dissemination of antibiotic resistance. An exciting challenge is to decipher the genetic and molecular basis of membrane impermeability as a bacterial resistance mechanism. This Review outlines the bacterial response towards antibiotic stress on altered membrane permeability and discusses recent advances in molecular approaches that are improving our knowledge of the physico-chemical parameters that govern the translocation of antibiotics through porin channels.
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            Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes.

            The three classes of enzymes which inactivate aminoglycosides and lead to bacterial resistance are reviewed. DNA hybridization studies have shown that different genes can encode aminoglycoside-modifying enzymes with identical resistance profiles. Comparisons of the amino acid sequences of 49 aminoglycoside-modifying enzymes have revealed new insights into the evolution and relatedness of these proteins. A preliminary assessment of the amino acids which may be important in binding aminoglycosides was obtained from these data and from the results of mutational analysis of several of the genes encoding aminoglycoside-modifying enzymes. Recent studies have demonstrated that aminoglycoside resistance can emerge as a result of alterations in the regulation of normally quiescent cellular genes or as a result of acquiring genes which may have originated from aminoglycoside-producing organisms or from other resistant organisms. Dissemination of these genes is aided by a variety of genetic elements including integrons, transposons, and broad-host-range plasmids. As knowledge of the molecular structure of these enzymes increases, progress can be made in our understanding of how resistance to new aminoglycosides emerges.
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              Performance stand- ards for antimicrobial susceptibility testing

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                Author and article information

                Journal
                Antibiotics (Basel)
                Antibiotics (Basel)
                antibiotics
                Antibiotics
                MDPI
                2079-6382
                26 May 2014
                June 2014
                : 3
                : 2
                : 216-232
                Affiliations
                [1 ]Department of Drug Sciences, University of Catania, Città Universitaria, viale A. Doria 6, I-95125 Catania, Italy; E-Mails: r.pignatello@ 123456unict.it (R.P.); antonio.leonardi@ 123456gmail.com (A.L.); puglisig@ 123456unict.it (G.P.)
                [2 ]NANO- i, Research Centre for Ocular Nanotechnology, Department of Drug Sciences, University of Catania, viale A. Doria 6, I-95125 Catania, Italy
                [3 ]Department of Biomedical Sciences, University of Catania, via Androne 83, I-95124 Catania, Italy; E-Mail: gpetroniopetronio@ 123456gmail.com
                [4 ]IRCCS San Raffaele Pisana, Via della Pisana 235, I-00163 Roma, Italy
                [5 ]Pharmaceutical Technology, Te.Far.T.I. group, Department of Life Sciences, University of Modena and Reggio Emilia, via Campi 183, I-41100 Modena, Italy; E-Mail: barbara.ruozi@ 123456unimore.it
                Author notes
                [* ]Author to whom correspondence should be addressed; E-Mail: furneri@ 123456unict.it ; Tel.: +39-095-250-4705.
                Article
                antibiotics-03-00216
                10.3390/antibiotics3020216
                4790386
                27025745
                71778983-a19e-4d36-bf14-744e03cc4be7
                © 2014 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 license ( http://creativecommons.org/licenses/by/3.0/).

                History
                : 18 February 2014
                : 29 April 2014
                : 14 May 2014
                Categories
                Article

                coevaporates,physical mixtures,ion-pairs,lipoamino acids,amphiphilicity,dsc,pxdr,antibacterial activity,mic,e. coli

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