Structure dynamics reveal key residues essential for the sense of 1‐dodecanol by Cydia pomonella pheromone binding protein 2 ( CpomPBP2 )

2020 ◽  
Vol 76 (11) ◽  
pp. 3667-3675 ◽  
Author(s):  
Zhen Tian ◽  
Yue Li ◽  
Tong Zhou ◽  
Xuan Ye ◽  
Ruichi Li ◽  
...  
Keyword(s):  
Binding Protein ◽  
Cydia Pomonella ◽  
Pheromone Binding Protein ◽  
Structure Dynamics ◽  
Key Residues

Key Residues Involved in the Interaction between Cydia pomonella Pheromone Binding Protein 1 (CpomPBP1) and Codlemone

2016 ◽  
Vol 64 (42) ◽  
pp. 7994-8001 ◽  
Author(s):  
Zhen Tian ◽  
Jiyuan Liu ◽  
Yalin Zhang
Keyword(s):  
Binding Protein ◽  
Cydia Pomonella ◽  
Pheromone Binding Protein ◽  
Key Residues

scholarly journals Responses of the Pheromone-Binding Protein of the Silk Moth Bombyx mori on a Graphene Biosensor Match Binding Constants in Solution

Sensors ◽  
2021 ◽  
Vol 21 (2) ◽  
pp. 499
Author(s):  
Caroline Bonazza ◽  
Jiao Zhu ◽  
Roger Hasler ◽  
Rosa Mastrogiacomo ◽  
Paolo Pelosi ◽  
...  
Keyword(s):  
Bombyx Mori ◽  
Binding Protein ◽  
Binding Constants ◽  
Isoamyl Acetate ◽  
The Other ◽  
Oxide Surface ◽  
Binding Assays ◽  
Pheromone Binding Protein ◽  
Silk Moth ◽  
Good Agreement

An electronic biosensor for odors was assembled by immobilizing the silk moth Bombyx mori pheromone binding protein (BmorPBP1) on a reduced graphene oxide surface of a field-effect transistor. At physiological pH, the sensor detects the B. mori pheromones, bombykol and bombykal, with good affinity and specificity. Among the other odorants tested, only eugenol elicited a strong signal, while terpenoids and other odorants (linalool, geraniol, isoamyl acetate, and 2-isobutyl-3-methoxypyrazine) produced only very weak responses. Parallel binding assays were performed with the same protein and the same ligands, using the common fluorescence approach adopted for similar proteins. The results are in good agreement with the sensor’s responses: bombykol and bombykal, together with eugenol, proved to be strong ligands, while the other compounds showed only poor affinity. When tested at pH 4, the protein failed to bind bombykol both in solution and when immobilized on the sensor. This result further indicates that the BmorPBP1 retains its full activity when immobilized on a surface, including the conformational change observed in acidic conditions. The good agreement between fluorescence assays and sensor responses suggests that ligand-binding assays in solution can be used to screen mutants of a binding protein when selecting the best form to be immobilized on a biosensor.

scholarly journals Expression of a pheromone-binding protein in insect cells using a baculovirus vector

1992 ◽  
Vol 203 (1-2) ◽  
pp. 161-166 ◽  
Author(s):  
Jurgen KRIEGER ◽  
Klaus RAMING ◽  
Glenn D. PRESTWICH ◽  
David FRITH ◽  
Silvia STABEL ◽  
...  
Keyword(s):  
Insect Cells ◽  
Binding Protein ◽  
Baculovirus Vector ◽  
Pheromone Binding Protein

Physicochemical Basis and Comparison of Two Type II Sex Pheromone Components Binding with Pheromone-Binding Protein 2 from Tea Geometrid, Ectropis obliqua

2018 ◽  
Vol 66 (50) ◽  
pp. 13084-13095 ◽  
Author(s):  
Xiao-Bin Fu ◽  
Ya-Li Zhang ◽  
Yi-Lei Qiu ◽  
Xin-Mi Song ◽  
Fan Wu ◽  
...  
Keyword(s):  
Sex Pheromone ◽  
Binding Protein ◽  
Type Ii ◽  
Pheromone Binding Protein ◽  
Sex Pheromone Components ◽  
Pheromone Components ◽  
Physicochemical Basis

scholarly journals A Pheromone-Binding Protein Mediates the Bombykol-Induced Activation of a Pheromone Receptor In Vitro

2006 ◽  
Vol 31 (6) ◽  
pp. 547-555 ◽  
Author(s):  
E. Grosse-Wilde
Keyword(s):  
Binding Protein ◽  
Pheromone Receptor ◽  
Pheromone Binding Protein

Odorant Binding by a Pheromone Binding Protein: Active Site Mapping by Photoaffinity Labeling

Biochemistry ◽  
1994 ◽  
Vol 33 (16) ◽  
pp. 4812-4819 ◽  
Author(s):  
Gehua Du ◽  
Chi-Shing Ng ◽  
Glenn D. Prestwich
Keyword(s):  
Active Site ◽  
Binding Protein ◽  
Photoaffinity Labeling ◽  
Pheromone Binding Protein ◽  
Site Mapping ◽  
Odorant Binding ◽  
Protein Active Site

Disulfide structure of the pheromone binding protein from the silkworm moth, Bombyx mori

FEBS Letters ◽  
1999 ◽  
Vol 464 (1-2) ◽  
pp. 85-90 ◽  
Author(s):  
Walter S Leal ◽  
Larisa Nikonova ◽  
Guihong Peng
Keyword(s):  
Bombyx Mori ◽  
Binding Protein ◽  
Pheromone Binding Protein ◽  
Disulfide Structure
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