Oostatic peptides containing D-amino acids: synthesis, oostatic activity, degradation, accumulation in ovaries and NMR study.

Analogs of the H-Tyr-Asp-Pro-Ala-Pro-OH pentapeptide with D-amino acid residues either in differing or in all of the positions of the sequences were prepared and their oostatic potency was compared with that of the parent pentapeptide. The D-amino acid residue containing analogs exhibited an equal or even higher oostatic effect in the flesh fly Neobellieria bullata than the parent peptide. Contrary to the rapid incorporation of radioactivity from the labeled H-Tyr-Asp-[3H]Pro-Ala-Pro-OH pentapeptide into the ovaries of N.

Distribution of a juvenogen and its metabolites in a laboratory system during juvenogen-induced caste differentiation in a termite, Reticulitermes santonensis (Isoptera: Rhinotermitidae).

Background: Juvenoids and juvenogens have been for many years considered promising candidates for control of pest insect species including termites. Their use as termite pest management agents requires the generation of knowledge concerning their degradation and distribution in time and space. Groups of 40 Reticulitermes santonensis de Feytaud workers were provided with wood impregnated with a juvenogen, ethyl cis-N-{2-[4-(2-butyryloxycyclohexylmethyl)phenoxy]ethyl}carbamate, labelled with tritium in the benzene ring (305 GBq mmol(-1)).

Radiochromatographic assay of metabolites of the oostatic peptide labeled in different positions of the peptide chain.

Reversed-phase high-performance liquid radio-chromatography (radio-HPLC) was set up to detect the time course of labeled degradation product formation of the pentapeptide H-Tyr-Asp-Pro-Ala-Pro-OH (5P), which has oostatic effects in different insect species. The detection limit of the system was in the range of 80-150 Bq. To follow formation of the degradation products, three amino acid residues in 5P were independently tritiated: Tyr1, Pro3 and Pro5.

Activity and mechanism of action of insect oostatic peptides in flesh fly.

The relationship between structure and activity of insect oostatic decapeptide (Aed-TMOF) analogues in flesh fly was analyzed. The highest oostatic activity was exhibited by the pentapetide and tetrapeptide analogues, H-Tyr-Asp-Pro-Ala-Pro-OH and H-Tyr-Asp-Pro-Ala-OH, respectively. The tetrapeptide, either native or tritiated, was used to study its metabolism in the ovaries and hemolymph and to detect putative binding sites in the flesh fly ovaries and head.