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

Hooper, A., Dufour, S., He, X., Muck, A., Zhou, J.-J., Almeida, R., Field, L., Svatoš, A. and Pickett, J. ORCID: https://orcid.org/0000-0002-8386-3770 2009. High-throughput ESI-MS analysis of binding between the Bombyx mori pheromone-binding protein BmorPBP1, its pheromone components and some analogues. Chemical Communications (38) , pp. 5725-5727. 10.1039/b914294k

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Abstract

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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Schools > Chemistry
Publisher:	Royal Society of Chemistry
ISSN:	1359-7345
Date of Acceptance:	20 August 2009
Last Modified:	18 Feb 2026 11:15
URI:	https://orca.cardiff.ac.uk/id/eprint/184928

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