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Biological evaluation of analogues of an insect neuropeptide proctolin.

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Woźnica I., Szeszel-Fedorowicz W., Rosiński G., Konopińska D.

Acta Biochimica Polonica

2004

vol. 51

issue 1

115-119

Continuing our studies on proctolin (Arg-Tyr-Leu-Pro-Thr) we performed the synthesis and biological evaluation of 52 analogues substituted in position 2, 3, 4, and 5 of the peptide chain. The peptides were bioassayed for cardiotropic activity in vitro on Tenebrio molitor and myotropic activity on foregut of Schistocerca gregaria. Twenty analogues retained 20-80% of proctolin activity.

Chelating ability of proctolin tetrazole analogue

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Łodyga-Chruścińska E., Sanna D., Micera G., Chruściński L., Olejnik J., Nachman R. J., Zabrocki J.

Acta Biochimica Polonica

2006

vol. 53

issue 1

65-72

The aim of the investigation was to establish the chelating ability of a new proctolin analogue of the sequence Arg-Tyr-LeuΨ[CN4]Ala-Thr towards copper(II) ions. The insertion of the tetrazole moiety into the peptide sequence has considerably changed the coordination ability of the ligand. Potentiometric and spectroscopic (UV-Vis, CD, EPR) results indicate that the incorporation of 1,5-disubstituted tetrazole ring favours the formation of a stable complex form of CuH-1L. This 4N coordination type complex is the dominant species in the physiological pH range. The tetrazole moiety provides one of these nitrogens. The data indicate that Cu(II) ions are strongly trapped inside the peptide backbone. These findings suggest that Cu(II) can hold peptide chains in a bent conformation. This bent conformation may be essential for bioactivity of the tetrazole peptides.

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2 Acta Biochimica Polonica

1 2006

1 2004

1 Chruściński L.

1 Konopińska D.

1 Micera G.

1 Nachman R. J.

1 Olejnik J.

1 Rosiński G.

1 Sanna D.

1 Szeszel-Fedorowicz W.

1 Woźnica I.

1 Zabrocki J.

1 Łodyga-Chruścińska E.

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Biological evaluation of analogues of an insect neuropeptide proctolin.

Chelating ability of proctolin tetrazole analogue