Design of histidine containing peptides for better understanding of their coordination mode toward copper(II) by CD spectroscopy.

Design of histidine containing peptides for better understanding of their coordination mode toward copper(II) by CD spectroscopy. Research Abstract Details 

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Design of histidine containing peptides for better understanding of their coordination mode toward copper(II) by CD spectroscopy. Abstract Text:

Jakab, Gyurcsik, ,Ilze Vosekalna,Jan Jensen,Erik Larsen, Jakab, Gyurcsik, ,Ilze Vosekalna,Jan Jensen,Erik Larsen,

The systematic investigation of the copper(II) complexes of tripeptides Xaa-Xaa-His, Xaa-His-Xaa and His-Xaa-Xaa, where Xaa=Gly or Ala was performed by combined pH-metry, spectrophotometry, CD and in part EPR spectroscopy. The matrix rank analysis of the spectral data revealed the number of the coloured and optically active species as a basis for the solution speciation. A critical evaluation on the speciation and solution structure of the complexes formed is presented on the basis of their d-d band optical activity. The replacement of a Gly residue with the chiral Ala amino acid allowed us to gain decisive information on the solution structure of the complexes by CD spectroscopy. It was shown that the tripeptides with histidine in the third position formed CuH(-2)L species with (NH(2), 2N(-), ImN - where Im stands for imidazole) coordination sphere as a major species, and only the macrochelated CuL complexes as minor species around pH 5.0. In copper(II)-Xaa-His-Xaa tripeptide systems the CuH(-1)L (NH(2), N(-), ImN) is the most stable species at physiological pH, but the vacant fourth site around copper(II)ions is offered for further deprotonation, most probably resulting in mixed hydroxo species at low (<5 x 10(-4)M) metal ion concentrations, while a tetrameric complex is dominant when the copper concentration exceeds 3 x 10(-3)M. The histamine type coordination mode in CuL and CuL(2) complexes of His-Xaa-Xaa ligands predominates at low pH. The structural consequences drawn from the CD spectra for the mono and bis parent complexes were supported by theoretical calculations. CD spectra strongly suggest the participation of the imidazole nitrogen both in the Cu(2)H(-2)L(2) and CuH(-2)L complexes.

Design of histidine containing peptides for better understanding of their coordination mode toward copper(II) by CD spectroscopy. Publishing Authors By Initials

NI Jakab,B Gyurcsik,T ,I Vosekalna,J Jensen,E Larsen,NI Jakab,B Gyurcsik,T ,I Vosekalna,J Jensen,E Larsen,

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Design of histidine containing peptides for better understanding of their coordination mode toward copper(II) by CD spectroscopy. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of inorganic biochemistry

VOLUME: 101

Page Numbers: 1376-85

Journal Abbreviation: J. Inorg. Biochem.

ISSN: 0162-0134

DAY: 2

MONTH: 06

YEAR: 2007

Design of histidine containing peptides for better understanding of their coordination mode toward copper(II) by CD spectroscopy. Information

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LANGUAGE: eng

NlmUniqueID: 7905788

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Grant and Affiliation Information for Design of histidine containing peptides for better understanding of their coordination mode toward copper(II) by CD spectroscopy.

AFFILIATION: Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 7, PO Box 440, H-6701 Szeged, Hungary.

Country: United States

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MEDLINETA: J Inorg Biochem

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