NDLI: The unusual stabilization of the $Ni^{2+}$ and $Cu^{2+}$ complexes with NSFRY

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Porciatti, Elena Remelli, Maurizio Valensin, Daniela Janicka-klos, Anna Kozlowski, Henryk Valensin, Gianni Conato, Chiara Oldziej, Stanislaw
Description	Author Affiliation: Janicka-Klos A ( Department of Inorganic Chemistry, Medical University of Wroclaw, Szewska 38, 50-139 Wroclaw, Poland. anna.janicka-kloss@am.wroc.pl)
Abstract	The binding mode provided by an unprotected peptide with non-coordinating side-chains is simple and well understood. However, when particular residues are inserted into the peptide sequence, they can have a significant impact on the stability of the formed complexes. The presence of non-bonding side chains of amino acids close to the metal binding centre in the peptide / protein can provide special interactions which result in increasing the stabilization of the formed species. Moreover, these interactions can play a crucial role in generating particular protein structures and in influencing biological activity. In the present paper it is shown how peptides with no specific predisposition for metal binding, like ANF peptides , can form metal complexes with a very high thermodynamic stability. For better understanding this peculiar behavior, a combined pH-metric and spectroscopic method was used to determine the stability and the solution structure of $Cu^{2+}$ and $Ni^{2+}$ complexes with $NSFRY-NH_{2}$ (ANF peptide ) and a series of analogue peptides . All obtained data support the hypothesis that the complex-formation process is very similar for both metal ions and all the ligands , involving some intramolecular interactions among the different side chains. The two-dimensional NMR analysis of nickel complexes showed the occurrence of many inter-residue correlations and suggested the presence of a direct interaction between the d electrons of the metal ion and the π-ring system of the aromatic side-chains of the ligand .
ISSN	14779226
Issue Number	2
Volume Number	42
e-ISSN	13645447
Journal	Dalton Trans.
Language	English
Publisher	Royal Society of Chemistry
Publisher Date	2013-01-14
Publisher Place	Great Britain (UK)
Access Restriction	Subscribed
Subject Keyword	Copper Chemistry Nickel Organometallic Compounds Peptide Fragments Amino Acid Sequence Atrial Natriuretic Factor Magnetic Resonance Spectroscopy Models, Molecular Molecular Conformation Protons Journal Article Research Support, Non-U.S. Gov't
Content Type	Text
Resource Type	Article
Subject	Inorganic Chemistry

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