http://www.cnr.it/ontology/cnr/individuo/prodotto/ID16200
Copper(II) complexes of rat amylin fragments. (Articolo in rivista)
- Type
- Label
- Copper(II) complexes of rat amylin fragments. (Articolo in rivista) (literal)
- Anno
- 2011-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1039/c1dt10835b (literal)
- Alternative label
C. Kállay, Á. Dávid, S. Timári, E. M. Nagy, D. Sanna, E. Garribba, G. Micera, P. De Bona, G. Pappalardo, E. Rizzarelli, I. Sóvágó (2011)
Copper(II) complexes of rat amylin fragments.
in Dalton transactions (2003. Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- C. Kállay, Á. Dávid, S. Timári, E. M. Nagy, D. Sanna, E. Garribba, G. Micera, P. De Bona, G. Pappalardo, E. Rizzarelli, I. Sóvágó (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Department of Inorganic and Analytical Chemistry, University ofDebrecen; CNR Institute of Biomolecular Chemistry; Department of Chemistry and Center for Biotechnology Development and Biodiversity Research; Department of Chemical Sciences, University of Catania; CNR Institute of Biostructures and Bioimagining. (literal)
- Titolo
- Copper(II) complexes of rat amylin fragments. (literal)
- Abstract
- The fragments of rat amylin rIAPP(17-29) (Ac-VRSSNNLGPVLPP-NH2), rIAPP(17-22)
(Ac-VRSSNN-NH2), rIAPP(19-22) (Ac-SSNN-NH2) and rIAPP(17-20) (Ac-VRSS-NH2) together
with the related mutant peptides (Ac-VASS-NH2 and Ac-VRAA-NH2) have been synthesized and their
copper(II) complexes studied by potentiometric, UV-Vis, CD and EPR spectroscopic methods. Despite
the lack of any common strongly coordinating donor functions some of these fragments are able to
bind copper(II) ions in the physiological pH range. The longest fragment rat amylin(17-29) keeps one
equivalent copper(II) ion in solution in the whole pH range, while two other peptides Ac-VRSSNN-NH2
and Ac-SSNN-NH2 are also able to interact with copper(II) ions in the slightly alkaline pH range.
According to the spectral parameters of the complexes, the peptides can be classified into two different
categories: (i) the tetrapeptides Ac-VRSS-NH2, Ac-VASS-NH2 and Ac-VRAA-NH2 can interact with
copper(II) only under strongly alkaline conditions (pH > 10.0) and the formation of only one species
with four amide nitrogen coordination can be detected; (ii) the peptides Ac-VRSSNNLGPVLPP-NH2,
Ac-VRSSNN-NH2 and Ac-SSNN-NH2 can form complexes above pH 6.0 with the major
stoichiometries [CuH-2L], [CuH-3L]- and [CuH-4L]2-. These data support that rIAPP(17-29) can
interact with copper(II) ions under physiological conditions and the SSNN tetrapeptide fragment can
be considered as the shortest sequence responsible for metal binding. Density functional theory (DFT)
calculations provide some information on the possible coordination modes of Ac-SSNN-NH2 towards
the copper(II) ion and suggest that for [CuH-2L], [CuH-3L]- and [CuH-4L]2-, the binding of two, three
and four deprotonated amide nitrogens, with NH- of the side chain of asparagine as anchoring group,
is probable. Moreover, these data reveal that peptides can be effective metal binding ligands even in the
absence of anchoring groups, if more polar side chains are present in a specific sequence. (literal)
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