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Effect of tetrazole moiety on coordinating efficiency of deltorphin.

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Łodyga-Chruścińska E., Ołdziej S., Micera G., Sanna D., Chruściński L., Olczak J., Zabrocki J.

Acta Biochimica Polonica

2004

vol. 51

issue 1

93-106

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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1 Acta Biochimica Polonica

1 2004

1 Chruściński L.

1 Micera G.

1 Olczak J.

1 Ołdziej S.

1 Sanna D.

1 Zabrocki J.

1 Łodyga-Chruścińska E.

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Effect of tetrazole moiety on coordinating efficiency of deltorphin.