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Structure and activity of Bombyx PBAN
H Nagasawa1, H Kuniyoshi, R Arima
1Department of Agricultural Chemistry, Faculty of Agriculture, University of Tokyo, Japan.
Archives of Insect Biochemistry and Physiology
|January 1, 1994
Summary
Two pheromone biosynthesis activating neuropeptides (PBANs) were identified in silkworms. Modifications to PBAN structure significantly enhanced activity and stability, impacting sex pheromone production.
Area of Science:
- Biochemistry
- Insect Physiology
- Molecular Endocrinology
Background:
- Pheromone biosynthesis activating neuropeptides (PBANs) regulate insect reproduction.
- Silkworm (Bombyx mori) PBANs, PBAN-I and -II, were previously uncharacterized.
- Understanding PBAN structure-activity relationships is crucial for insect communication research.
Purpose of the Study:
- To isolate and characterize PBAN-I and -II from Bombyx mori.
- To elucidate the structure-activity relationships of PBANs.
- To investigate the cross-activity between PBANs and myotropic peptides.
Main Methods:
- Peptide isolation and characterization from adult silkworm heads.
- Structure-activity relationship studies involving peptide modifications.
- Cross-activity assays with myotropic peptides from locusts and cockroaches.
Main Results:
- PBAN-I, a 33-residue peptide, was characterized with a crucial carboxyl-terminal amide.
- Oxidation of methionine residues enhanced PBAN-I activity; N-terminal modification increased stability.
- PBANs showed myotropic activity, while myotropic peptides exhibited high pheromonotropic activity.
Conclusions:
- The carboxyl-terminal pentapeptide and amide are essential for PBAN activity.
- Structural modifications, including N-terminal group alteration and methionine oxidation, enhance PBAN efficacy and stability.
- PBANs play a key role in activating sex pheromone biosynthesis in Bombyx mori.