Simple molecular model for the binding of antibiotic molecules to bacterial ion channels
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Simple molecular model for the binding of antibiotic molecules to bacterial ion channels

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Simple molecular model for the binding of antibiotic molecules to bacterial ion channels

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dc.contributor.author Mafé, Salvador
dc.contributor.author Ramírez Hoyos, Patricio
dc.contributor.author Alcaraz, Antonio
dc.date.accessioned 2010-07-28T11:42:41Z
dc.date.available 2010-07-28T11:42:41Z
dc.date.issued 2003
dc.identifier.uri http://hdl.handle.net/10550/16694
dc.language.iso en en
dc.relation http://scitation.aip.org/getpdf/servlet/GetPDFServlet?filetype=pdf&id=JCPSA6000119000015008097000001&idtype=cvips&prog=normal&doi=10.1063/1.1606438 en
dc.source MAFÉ, Salvador ; RAMÍREZ, Patricio ; ALCARAZ, Antonio. Simple molecular model for the binding of antibiotic molecules to bacterial ion channels. En: Journal of Chemical Physics, 2003, vol. 119, no. 15 en
dc.subject Microorganisms ; Bonds (Chemical) ; Intermolecular Mechanics ; Biochemistry ; Molecular Biophysics ; pH en
dc.title Simple molecular model for the binding of antibiotic molecules to bacterial ion channels en
dc.type info:eu-repo/semantics/article en
dc.type info:eu-repo/semantics/publishedVersion en
dc.subject.unesco UNESCO::QUÍMICA::Química física en
dc.identifier.doi 10.1063/1.1606438 en
dc.description.abstractenglish A molecular model aimed at explaining recent experimental data by Nestorovich et al. [Proc. Natl. Acad. Sci. USA 99, 9789 (2002)] on the interaction of ampicillin molecules with the constriction zone in a channel of the general bacterial porin, OmpF (outer membrane protein F), is presented. The model extends T. L. Hill’s theory for intermolecular interactions in a pair of binding sites [J. Am. Chem. Soc. 78, 3330 (1956)] by incorporating two binding ions and two pairs of interacting sites. The results provide new physical insights on the role of the complementary pattern of the charge distributions in the ampicillin molecule and the narrowest part of the channel pore. Charge matching of interacting sites facilitates drug binding. The dependence of the number of ampicillin binding events per second with the solution pH and salt concentration is explained qualitatively using a reduced number of fundamental concepts. en
dc.description.private Salvador.Mafé@uv.es en
dc.identifier.idgrec 002529 en

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