Lodyga-Chruscinska, Elzbieta and Oldziej, Stanislaw and Micera, Giovanni and Sanna, Daniele and Chruscinski, Longin and Olczak, Jacek and Zabrocki, Janusz (2004) Effect of tetrazole moiety on coordinating efficiency of deltorphin. Acta Biochimica Polonica, Vol. 51 (1), p. 93-106. ISSN 1734-154X. Article.
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A study of the effect of the tetrazole moiety, a cis-amide bond surrogate, on the Cu(II) coordinating properties of oligopeptides is reported. Insertion of the tetrazole moiety Ψ[CN4] into the peptide sequence of [D-Ala2]deltorphin I changes considerably the coordination ability of the peptide. Potentiometric and spectroscopic results show that if the tetrazole moiety is in a suitable position in the peptide chain, i.e. it follows the second residue, a stable CuL species involving 3N coordination is formed in the physiological pH range. The tetrazole Ψ[CN4] ring provides one of these nitrogens. The data indicate that Cu(II) ions are strongly trapped inside a bent peptide backbone. The peptide conformation changes achieved by Cu(II) coordination may be essential for the binding of tetrazole deltorphins at opiate receptors.
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