High-throughput ESI-MS analysis of binding between the Bombyx mori pheromone-binding protein BmorPBP1, its pheromone components and some analogues.
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.
Rothamsted Research, Department of Biological Chemistry, West Common, Harpenden, Hertfordshire, UK AL5 2JQ. tony.hooper@bbsrc.ac.uk
Antony M
AM
Hooper
Samuel
S
Dufour
Xaoli
X
He
Alexander
A
Muck
Jing-Jiang
JJ
Zhou
Reinaldo
R
Almeida
Linda M
LM
Field
Ales
A
Svatos
John A
JA
Pickett
D000466:Alkadienes / Q000737:chemistry; D000818:Animals; D012831:Bombyx / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D005233:Fatty Alcohols / Q000737:chemistry; D019476:Insect Proteins / Q000737:chemistry*; D036341:Intercellular Signaling Peptides and Proteins; D010675:Pheromones / Q000737:chemistry*; D011485:Protein Binding; D021241:Spectrometry, Mass, Electrospray Ionization
D000466:Alkadienes; D002352:Carrier Proteins; D005233:Fatty Alcohols; D019476:Insect Proteins; D036341:Intercellular Signaling Peptides and Proteins; D010675:Pheromones; C403094:pheromone-binding protein, Bombyx; C066482:bombykal; C006787:bombykol