Activity and mechanism of action of insect oostatic peptides in flesh fly
| Autor: | Petr Šimek, Jirina Slaninova, Elšan S. Nazarov, Jan Hlaváček, Věra Vlasáková, Blanka Bennettová, Bohuslav Černý, Richard Tykva, Josef Holík |
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| Rok vydání: | 2004 |
| Předmět: |
Insecta
medicine.medical_treatment Biochemistry Hemolymph Drug Discovery medicine Animals Pharmacokinetics Protease Inhibitors Binding site Tyrosine Molecular Biology Binding Sites Protease Tetrapeptide biology Chemistry Flesh fly Diptera Ovary fungi Organic Chemistry Metabolism biology.organism_classification Peptide Fragments Biodegradation Environmental Mechanism of action Female medicine.symptom Head Oligopeptides |
| Zdroj: | Bioorganic Chemistry. 32:263-273 |
| ISSN: | 0045-2068 |
| DOI: | 10.1016/j.bioorg.2004.05.003 |
| Popis: | 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. A high metabolism of the tetrapeptide with a half-life in the hemolymph and ovaries less than 1 h was determined. The initial limiting step in the degradation is tyrosine 1 cleavage. Other degradation products were detected only transiently in low quantities. Using tritiated tetrapeptide, we found that only very low specific binding was detected in the homogenates of ovaries and in the rough membrane preparation in the presence and absence of protease inhibitors. |
| Databáze: | OpenAIRE |
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