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2 Polish Journal of Chemistry

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The Role of Histidine Residue in Coordination Abilities of Peptides with Multi Histidine Sequence Towards Nickel(II) Ions

Matera A., Brasuń J., Cebrat M., Świątek-Kozłowska J.

Polish Journal of Chemistry

2008

Vol. 82, nr 7

1367-1367

Previous studies on the histidine rich pep tides-Cu2+ systems have shown very efficient coordination abilities and high termodynamic stability of the complexes formed. In this work the ability of histidine-rich peptides with Ni2+ ions are presented. The coordination abilities of the series of the N-protected (Ac-His-Arg-His-Gly-His-Gly, Ac-His-Gly-His-Arg-His-Gly, Ac-Gly-His-His-Arg-His-Gly, Ac-His-His-Gly-His-Arg-Gly) and unprotected peptides (His-Arg-His-Gly-His-Gly, His-Gly-His-Arg-His-Gly, Gly-His-His-Arg-His-Gly, and His-His-Gly-His-Arg-Gly) towards Ni2+ ions were studied by spectroscopic (UV/VIS, CD) and potentiometric methods. For the N-protected peptides the dominant complex species with {3Nim} in physiological pH range has been determined, while for the unprotected peptides the coordination of the first amide nitrogen takes place. More over, for the Ni2+-peptide systems the complexes with two geometries were determined: the paramagnetic octahedral species within the acidic pH range and the diamagnetic square-planar species at pH exceeding 7.

Specific Interactions of Cu2+ Ions with Enantiomers of Hepatitis B Virus Surface Antigen 140-146 Region

Świątek-Kozłowska J., Brasuń J., Maćkiewicz Z., Kupryszewski G.

Polish Journal of Chemistry

2001

Vol. 75, nr 6

813-822

Potentiometric and spectroscopic studies on Cu(II) interactions with 140-146 fragment of the hepatitis B virus antigen have shown that the basic binding sites of metal ion are centered at a peptide N-terminal donor system and the side chain donor atoms are not competing in the metal ion coordination.