Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5088
DC FieldValueLanguage
dc.contributor.authorSwiatek, Men_us
dc.contributor.authorValensin, Danielaen_us
dc.contributor.authorMigliorini, Caterinaen_us
dc.contributor.authorGaggelli, Elenaen_us
dc.contributor.authorValensin, Giannien_us
dc.contributor.authorJEZOWSKA BOJCZUK, M.en_us
dc.date.accessioned2021-03-30T15:48:57Z-
dc.date.available2021-03-30T15:48:57Z-
dc.date.issued2005-
dc.identifier.issn1477-9226en_US
dc.identifier.urihttp://hdl.handle.net/20.500.12779/5088-
dc.description36347en_US
dc.description.abstractVancomycin, a “last chance” antibiotic, is a glycopeptide consisting of an oligopeptide unit being potentially the effective binder of Cu2+ ions. The potentiometric and spectroscopic studies (UV-Vis, CD, EPR, NMR) have shown that, indeed, the peptide unit binds cupric ions very effectively forming almost instantly the 3N complex involving the N-terminal nitrogen donors in the metal ion coordination. The comparison of the binding ability of vancomycin with other peptide chelators clearly shows the efficiency of this antibiotic in metal ion coordination. It is very likely that Cu2+ ions may play a crucial role in the pharmacology of vancomycin, particularly when administered in high doses.en_US
dc.language.isoenen_US
dc.relationNoneen_US
dc.relation.ispartofDALTON TRANSACTIONSen_US
dc.titleUnusual binding ability of vancomycin towards Cu2+ ions.en_US
dc.typeArticleen_US
dc.identifier.doi10.1039/b508662ken_US
dc.identifier.scopus2-s2.0-29144504977en_US
dc.identifier.isiWOS:000233744200016en_US
dc.relation.volume2005en_US
dc.description.firstpage3808en_US
dc.description.lastpage3813en_US
dc.description.thirdmissionNot applicableen_US
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeArticle-
item.fulltextNo Fulltext-
crisitem.author.orcid0000-0003-4187-3919-
crisitem.author.orcid9810-
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