The effect of ring size of fused chelates on the stability constants and spectroscopic properties of nickel(II) and palladium(II) complexes of peptides

Ágoston, Csaba Gábor; Miskolczy, Zsombor; Nagy, Zoltán; Sóvágó, Imre

doi:10.1016/s0277-5387(03)00367-x

Cited by 17 publications

(4 citation statements)

References 19 publications

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“…These values are between 8.6 and 9.4, which means that the formation of NiL complexes shifts the deprotonation of amide nitrogens to higher pH range (e.g. for oligoglycines: (Gly) 4 : pK av (amide) = 7.9, 24 (Gly) 3 : pK av = 8.3 25 ).…”

Section: Nickel(ii) Complexesmentioning

confidence: 99%

Transition metal complexes of short multihistidine peptides

et al. 2009

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Nickel(ii), cobalt(ii) and cadmium(ii) complexes of terminally protected multihistidine peptides including Ac-HGH-OH, Ac-HGH-NHMe, Ac-HHGH-OH, Ac-HAHVH-NH(2), Ac-HVHGH-NH(2), Ac-HGHVH-NH(2) and Ac-(His-Sar)(n)-His-NH(2) (n = 1, 2 or 3) were studied by potentiometric, UV-Vis, CD and (1)H NMR spectroscopic techniques. It was found that the complexes in which the histidine imidazole nitrogens coordinate with ML stoichiometry are the main species in the physiological pH-range in all cases. The stability of these complexes is determined by the number of bound imidazole rings, the presence of the carboxylate group and the quality of the metal ion centre. The larger the number of coordinated imidazole-N donor atoms, the higher the stability of the complex. The stability constants of the ML complexes follow the Ni(ii) > Co(ii) approximately Cd(ii) order. Cobalt(ii) and cadmium(ii) are not, but nickel(ii) is able to promote the deprotonation and the coordination of amide nitrogens and NiH(-2)L and NiH(-3)L (Ni(2)H(-4)L) species predominate in basic solutions. For the pentapeptides with the exception of the sarcosine containing ligand the presence of coordination isomers is supported by spectroscopic methods. These data reveal that the favoured isomers are coordinated on the C-termini, but the ratio of isomers depends on the sequence of peptides.

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Section: Nickel(ii) Complexesmentioning

confidence: 99%

Transition metal complexes of short multihistidine peptides

et al. 2009

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“…The insertion of β-alanine into the peptide sequence changes the number of atoms within the chelates from fi ve to six in the peptide complexes. In the case of nickel(II) this change does not affect the speciation and the basic coordination modes, but the overall stability of the complexes of dipeptides with (NH 2 , N Ϫ , COO Ϫ ) and tripeptides with (NH 2 , N Ϫ , N Ϫ , COO Ϫ ) coordination modes follows the stability order: (5,5) ϳ (5,6) Ͼ (6,5) Ͼ (6,6) and (5,5,6) Ն (5,6,5) Ն (5,5,5) Ͼ (6,5,5) Ͼ (5,6,6) Ͼ (6,5,6) Ͼ (6,6,6), respectively [83].…”

Section: Nickel(ii) Complexes Of Peptides With Non-coordinating Side mentioning

confidence: 99%

Nickel Ion Complexes of Amino Acids and Peptides

Kowalik-Jankowska

Kozłowski

Farkas

et al. 2007

Nickel and Its Surprising Impact in Nature

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“…On the other hand, the introduction of an histidine amino-acid leads to an increase of the complexation ability of the dipeptide (Gly-His [25], Pro-His [26]), which can be explained by the presence of the imidazol group in C-terminal position. Whereas in the case of the Ni(II) metallic cation the ProThr dipeptide is less coordinating than the other dipeptides [27][28][29] (Fig. 5b).…”

Section: Potentiometric Studymentioning

confidence: 97%