Binding of Oxovanadium(IV) to Tripeptides Containing Histidine and Cysteine Residues and Its Biological Implication in the Transport of Vanadium and Insulin-Mimetic Compounds. (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Binding of Oxovanadium(IV) to Tripeptides Containing Histidine and Cysteine Residues and Its Biological Implication in the Transport of Vanadium and Insulin-Mimetic Compounds. (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1002/ejic.200500304 (literal)

Alternative label

• E. Garribba; G. Micera; E. Lodyga-Chruscinska; D. Sanna; G. Sanna (2005)
  Binding of Oxovanadium(IV) to Tripeptides Containing Histidine and Cysteine Residues and Its Biological Implication in the Transport of Vanadium and Insulin-Mimetic Compounds.
  in European journal of inorganic chemistry (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• E. Garribba; G. Micera; E. Lodyga-Chruscinska; D. Sanna; G. Sanna (literal)

Pagina inizio

• 4953 (literal)

Pagina fine

• 4963 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

• http://onlinelibrary.wiley.com/doi/10.1002/ejic.200500304/abstract (literal)

Rivista

• European journal of inorganic chemistry (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Department of Chemistry, University of Sassari,Via Vienna 2, I-07100 Sassari, Italy Institute of General Food Chemistry, Technical University of Lodz, ul. Stefanowskiego 4/10, PL-90924 Lodz, Poland Istituto C. N. R. di Chimica Biomolecolare, Trav. La Crucca 3, 07040 Li Punti, Sassari, Italy (literal)

Titolo

• Binding of Oxovanadium(IV) to Tripeptides Containing Histidine and Cysteine Residues and Its Biological Implication in the Transport of Vanadium and Insulin-Mimetic Compounds. (literal)

Abstract

• The complexation of the oxovanadium(IV) ion with five dipeptides containing L-histidine or L-cysteine (GlyHis, HisHis, HisGly, CysGly, GlyCys) was studied. L-histidinamide (HisNH2) was assumed as a model system for dipeptides with L-histidine in the N-terminal position. The study was performed in aqueous solution through the combined application of potentiometric and spectroscopic (electronic absorption and EPR) techniques. The results indicate that simple dipeptides lacking a strong anchoring group can form mono- and bischelated complexes with the VIVO ion if a suitable \"donor\" is present in the chain. The ligands behave like amino acids in the acidic and neutral pH range, inhibit the precipitation of hydroxides and suppress the formation of hydrolytic species if at least a fivefold molar excess of ligand is used. In alkaline media all the ligands, except CysGly, promote the deprotonation and N-coordination of the amide group. CysGly forms a bischelated complex with a [2 (NH2, S-)] donor set. The contribution of the deprotonated amide group to the 51V hyperfine coupling constant, Az, as a function of the total equatorial charge of oxovanadium(IV) ion, is discussed. The results have general validity and are useful to predict the geometry and donor set of complexes involving the bonding of the VIVO ion to the deprotonated amide group. (literal)

Prodotto di

• Caratterizzazione di complessi metallici formati da proteine coinvolte in patologie correlate al disordine conformazionale proteico. (PM.P01.004.002) (Modulo)
• Institute of biomolecular chemistry (ICB) (Istituto)

Autore CNR

• DANIELE SANNA (Unità di personale interno)

Incoming links:

Autore CNR di

• DANIELE SANNA (Unità di personale interno)

Prodotto

• Institute of biomolecular chemistry (ICB) (Istituto)
• Caratterizzazione di complessi metallici formati da proteine coinvolte in patologie correlate al disordine conformazionale proteico. (PM.P01.004.002) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• European journal of inorganic chemistry (Rivista)