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Chem. Commun., 2009, 5725 - 5727, DOI: 10.1039/b914294k

High-throughput ESI-MS analysis of binding between the Bombyx mori pheromone-binding protein BmorPBP1, its pheromone components and some analogues

Antony M. Hooper, Samuel Dufour, Xaoli He, Alexander Muck, Jing-Jiang Zhou, Reinaldo Almeida, Linda M. Field, Ale Svato and John A. Pickett

Chip-assisted high-throughput ESI-MS analysis of the pheromone-binding protein of the silkworm moth Bombyx mori, BmorPBP1, incubated with its pheromone components bombykol, bombykal and analogues was developed. The protein bound to bombykol ((10E,12Z)-hexadecadien-1-ol) and all 3 of its geometric isomers to a lesser extent, and showed relaxed specificity toward different chain lengths possessing unsaturation. BmorPBP1 did not bind to bombykal ((10E,12Z)-hexadecadienal), demonstrating molecular recognition of the insect pheromone components.

Graphical abstract image for this article (ID: b914294k)