Discovery of a linear lead antagonist to the insect pheromone biosynthesis activating neuropeptide (PBAN)☆
| Autor: | Chaim Gilon, Miriam Altstein, Irina Zeltser, Orna Ben-Aziz, Irit Schefler |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Physiology
Moths Biology Biochemistry Pheromones Cellular and Molecular Neuroscience chemistry.chemical_compound Endocrinology Biosynthesis Peptide Library Animals Amino Acid Sequence Peptide library Peptide sequence chemistry.chemical_classification Neuropeptides Antagonist biology.organism_classification Peptide Fragments Amino acid chemistry Sex pheromone Pheromone biosynthesis activating neuropeptide Female Heliothis peltigera Oligopeptides |
| Zdroj: | Peptides. 21:1457-1465 |
| ISSN: | 0196-9781 |
| DOI: | 10.1016/s0196-9781(00)00298-9 |
| Popis: | We report the discovery of a linear lead antagonist for the insect pheromone biosynthesis activating neuropeptide (PBAN) which inhibits sex pheromone biosynthesis in the female moth Heliothis peltigera. Two approaches have been used in attempting to convert PBAN agonists into antagonists. The first involved omission of the C-terminal amide and reduction of the sequence from the N-terminus in a linear library based on PBAN 1-33NH(2.) The second involved replacement of L amino-acids by the D hydrophobic amino acid D-Phe in a linear library based on PBAN28-33NH(2.) Screening of the two libraries for pheromonotropic antagonists resulted in the disclosure of one compound out of the D-Phe library (Arg-Tyr-Phe-D-Phe-Pro-Arg-Leu-NH(2)) which inhibited sex pheromone production by 79 and 64% at 100 pmol in two moth colonies and exhibited low agonistic activity. Omission of the C-terminal amide in PBAN 1-33NH(2) and its shorter analogs did not lead to the discovery of an antagonistic compound. |
| Databáze: | OpenAIRE |
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