Title: | Selective and pH-dependent binding of a moth pheromone to a pheromone-binding protein |
Author(s): | Leal WS; Chen AM; Erickson ML; |
Address: | "Maeda-Duffey Laboratory, Department of Entomology, University of California, Davis, CA 95616, USA. wsleal@ucdavis.edu" |
DOI: | 10.1007/s10886-005-7458-4 |
ISSN/ISBN: | 0098-0331 (Print) 0098-0331 (Linking) |
Abstract: | "Fluorescence and circular dichroism (CD) data suggest that the major pheromone-binding protein (PBP) from the wild silkmoth, Antheraea polyphemus, ApolPBP1, undergoes a pH-dependent conformational change similar to that previously observed for the PBP from the silkworm moth, Bombyx mori, BmorPBP. All three constituents of the sex pheromone, E6,Z11-16Ac, E6,Z11-16Ald, and E4,Z9-14Ac, bound to ApolPBP1 with apparent high affinity at high pH, but reduced binding at low pH when tested individually in a 'cold binding assay.' In competitive assays, however, ApolPBP1 showed considerable preference for the major constituent of the sex pheromone, E6,Z11-16Ac. These data suggest that specificity of PBPs contributes at least in part to the remarkable selectivity of moth's olfactory system" |
Keywords: | Animals Carrier Proteins/chemistry/*metabolism Circular Dichroism *Hydrogen-Ion Concentration Insect Proteins/chemistry/*metabolism Intercellular Signaling Peptides and Proteins Moths/*chemistry/metabolism Pheromones/chemistry/*metabolism Protein Binding; |
Notes: | "MedlineLeal, Walter S Chen, Angela M Erickson, Melissa L eng 2005/09/01 J Chem Ecol. 2005 Oct; 31(10):2493-9. doi: 10.1007/s10886-005-7458-4. Epub 2005 Sep 28" |