(Z)-9-tetradecenyl acetate, shows strongerin silicobinding to the pheromone-binding protein ofLobesia botranathan the major sex pheromone component

2016 ◽  
Author(s):  
Ana A Mutis
Keyword(s):  
Sex Pheromone ◽  
Binding Protein ◽  
Pheromone Component ◽  
Pheromone Binding Protein ◽  
Tetradecenyl Acetate

Generation of Polyclonal Antibody for Bombyx mori Pheromone-Binding Protein 1 (BmPBP1)

2013 ◽  
Vol 796 ◽  
pp. 15-20
Author(s):  
Kai Zun Xu ◽  
Ming Hui Wang ◽  
Lie Ma ◽  
Guo Sheng Li ◽  
Chao Mei ◽  
...  
Keyword(s):  
Sex Pheromone ◽  
Bombyx Mori ◽  
Polyclonal Antibody ◽  
Binding Protein ◽  
Information Communication ◽  
Male And Female ◽  
Odorant Binding Proteins ◽  
Pheromone Binding Protein ◽  
Moth Antenna ◽  
Odorant Binding

Bombyx mori pheromone-Binding Protein 1 (BmPBP1) in male moth antennae is a class of Odorant-Binding Proteins (OBPs), it can bind with the specific sex pheromone from female moth, thus initiates the males behaviors like seeking and mating, etc. It has been found that sex pheromone-binding protein 1 is differentially expressed in the antenna of male and female silkworm moths, however, the molecular mechanism of different PBP1 expression and its role in the information transmission are unclear. In this study, we successfully generated the BmPBP1 polyclonal antibody and used it to detect BmPBP1 expression in the silkworm moth antenna. Thus this work is helpful for further studies on the function of BmPBP1 in the information communication between male and female moths.

scholarly journals Responses of the Pheromone-Binding Protein of the Silk Moth Bombyx mori on a Graphene Biosensor Match Binding Constants in Solution

Sensors ◽  
2021 ◽  
Vol 21 (2) ◽  
pp. 499
Author(s):  
Caroline Bonazza ◽  
Jiao Zhu ◽  
Roger Hasler ◽  
Rosa Mastrogiacomo ◽  
Paolo Pelosi ◽  
...  
Keyword(s):  
Bombyx Mori ◽  
Binding Protein ◽  
Binding Constants ◽  
Isoamyl Acetate ◽  
The Other ◽  
Oxide Surface ◽  
Binding Assays ◽  
Pheromone Binding Protein ◽  
Silk Moth ◽  
Good Agreement

An electronic biosensor for odors was assembled by immobilizing the silk moth Bombyx mori pheromone binding protein (BmorPBP1) on a reduced graphene oxide surface of a field-effect transistor. At physiological pH, the sensor detects the B. mori pheromones, bombykol and bombykal, with good affinity and specificity. Among the other odorants tested, only eugenol elicited a strong signal, while terpenoids and other odorants (linalool, geraniol, isoamyl acetate, and 2-isobutyl-3-methoxypyrazine) produced only very weak responses. Parallel binding assays were performed with the same protein and the same ligands, using the common fluorescence approach adopted for similar proteins. The results are in good agreement with the sensor’s responses: bombykol and bombykal, together with eugenol, proved to be strong ligands, while the other compounds showed only poor affinity. When tested at pH 4, the protein failed to bind bombykol both in solution and when immobilized on the sensor. This result further indicates that the BmorPBP1 retains its full activity when immobilized on a surface, including the conformational change observed in acidic conditions. The good agreement between fluorescence assays and sensor responses suggests that ligand-binding assays in solution can be used to screen mutants of a binding protein when selecting the best form to be immobilized on a biosensor.

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