Equilibrium and structural studies on copper(II) complexes of tetra-, penta- and hexa-peptides containing histidyl residues at the C-termini

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dc.contributor.authorVarnagy, K.en
dc.contributor.authorSzabo, J.en
dc.contributor.authorSovago Ien
dc.contributor.authorMalandrinos, G.en
dc.contributor.authorHadjiliadis, N.en
dc.contributor.authorSanna, D.en
dc.contributor.authorMicera, G.en
dc.date.accessioned2015-11-24T16:57:56Z
dc.date.available2015-11-24T16:57:56Z
dc.identifier.issn1472-7773-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10635
dc.rightsDefault Licence-
dc.subjectnuclear-magnetic-resonanceen
dc.subjectglycylglycyl-l-histidineen
dc.subjectmetal-ion complexesen
dc.subjectimidazole nitrogensen
dc.subjectangiotensin-iien
dc.subjecttransport siteen
dc.subjectserum-albuminen
dc.subjectaminoen
dc.subjectoligopeptidesen
dc.subjectprotonen
dc.titleEquilibrium and structural studies on copper(II) complexes of tetra-, penta- and hexa-peptides containing histidyl residues at the C-terminien
heal.abstractThe stoichiometry, stability constants and solution structure of the complexes formed in the reaction of copper(II) with oligopeptides containing histidyl residues at the C-termini (Gly(3)His, Gly(4)His and Gly(5)His) have been determined by potentiometric, UV-VIS and EPR spectroscopic methods. The formation of the species [CuHL](2+), [CuL](+), [CuH(-1)L], [CuH(-2)L](-) and [CuH(-3)L](2-) was detected in all cases. Binding modes of the species [CuL](+), [CuH(-1)L] and [CuH(-2)L](-) were characterized by the metal ion co-ordination of the terminal amino group, carbonyl oxygen or one or two deprotonated amide nitrogens in joined five-membered chelates from the N-termini, while the fourth co-ordination site of the metal ion was occupied by nitrogen donors of imidazole in the form of a macrochelate. The stability of the macrochelate was decreased upon increasing the length of the peptide molecule. For the penta- and hexa-peptides the species [CuH(-3)L](2-) was characterized as a 4N-complex with equatorial co-ordination of the terminal amino group and subsequent three deprotonated amide nitrogens, with unco-ordinated imidazolyl residues, while a 5N-species was suggested to form for Gly(3)His with axial interaction of the imidazole-N donor atom. Copper(II) complexes of Gly(2)His and pentaglycine were also investigated for reliable comparison.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondary<Go to ISI>://000085350300007-
heal.journalNameJournal of the Chemical Society-Dalton Transactionsen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2000-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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