| Title: | Binding interaction between a queen pheromone component HOB and pheromone binding protein ASP1 of Apis cerana |
| Author(s): | Weng C; Fu Y; Jiang H; Zhuang S; Li H; |
| Address: | "Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, College of Life Sciences, China Jiliang University, Hangzhou 310018, China. College of Chemical Engineering, Zhejiang University of Technology, Hangzhou 310014, China. College of Environmental and Resource Sciences, Zhejiang University, Hangzhou 310058, China. Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, College of Life Sciences, China Jiliang University, Hangzhou 310018, China. Electronic address: hlli@cjlu.edu.cn" |
| DOI: | 10.1016/j.ijbiomac.2014.08.046 |
| ISSN/ISBN: | 1879-0003 (Electronic) 0141-8130 (Linking) |
| Abstract: | "The honeybee's social behavior is closely related to the critical response to pheromone, while pheromone binding proteins (PBPs) play an important role in binding and transferring those pheromones. Here we report one known PBP, antennal special protein 1(ASP1), which has high affinity with a queen mandibular pheromone component, methyl-p-hydroxybenzoate (HOB). In this study, multiple fluorescent spectra, UV absorption spectra, circular dichroism (CD) spectra and molecular docking analysis were combined to clarify the binding process. Basically, fluorescence intensity of ASP1 could be considerably quenched by HOB with an appropriate interaction distance (3.1 nm), indicating that a complex, which is more stable in lower temperature, was formed. The fact DeltaH < 0, DeltaS < 0, by thermodynamic analysis, indicated the van der Waals and hydrogen bond as main driving force. Moreover, synchronous fluorescence spectra and CD spectra analysis showed the change of partial hydrophilicity of ASP1 and the increase of alpha-helix after HOB addition. In conclusion, ASP1 can strongly and spontaneously interact with HOB. But the binding ability decreases with the rise of temperature, which may be necessary for sufficient social stability of hives. This study provides elucidation of the detailed binding mechanism and potential physicochemical basis of thermal stability to the social behavior of honeybee" |
| Keywords: | Animals Bees Carrier Proteins/chemistry/*metabolism Circular Dichroism Hydrophobic and Hydrophilic Interactions Hydroxybenzoates/*chemistry/metabolism Insect Proteins/chemistry/*metabolism Molecular Docking Simulation Pheromones/chemistry/*metabolism Prot; |
| Notes: | "MedlineWeng, Chen Fu, Yuxia Jiang, Hongtao Zhuang, Shulin Li, Hongliang eng Research Support, Non-U.S. Gov't Netherlands 2014/09/10 Int J Biol Macromol. 2015 Jan; 72:430-6. doi: 10.1016/j.ijbiomac.2014.08.046. Epub 2014 Sep 4" |
