Potentiometric and spectroscopic studies on the copper(II) complexes of rat amylin fragments. the anchoring ability of specific non-coordinating side chains

Ágnes Dávid, Csilla Kállay, Daniele Sanna, Norbert Lihi, Imre Sóvágó, Katalin Várnagy

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7 Citations (Scopus)

Abstract

Copper(ii) complexes of peptides modelling the sequence of the 17-22 residues of rat amylin have been studied by potentiometric, UV-Vis, CD and ESR spectroscopic methods. The peptides were synthesized in N-terminally free forms, NH2-VRSSNN-NH2, NH2-VRSSAA-NH2, NH2-VRAANN-NH2, NH2-VRSS-NH2, NH2-SSNN-NH2, NH2-SSNA-NH2 and NH2-AANN-NH2, providing a possibility for the comparison of the metal binding abilities of the amino terminus and the -SSNN- domain. The amino terminus was the primary ligating site in all cases and the formation of only mononuclear complexes was obtained for the tetrapeptides. The thermodynamic stability of the (NH2, N-, N-) coordinated complexes was, however, enhanced by the asparaginyl moiety in the case of NH2-SSNN-NH2, NH2-SSNA-NH2 and NH2-AANN-NH2. Among the hexapeptides the formation of dinuclear complexes was characteristic for NH2-VRSSNN-NH2 demonstrating the anchoring ability of the -SSNN- (SerSerAsnAsn) domain. The complexes of the heptapeptide NH2-GGHSSNN-NH2 were also studied and the data supported the above mentioned anchoring ability of the -SSNN- site.

Original languageEnglish
Pages (from-to)17091-17099
Number of pages9
JournalDalton Transactions
Volume44
Issue number39
DOIs
Publication statusPublished - Sep 3 2015

ASJC Scopus subject areas

  • Inorganic Chemistry

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