scholarly journals The Structural Properties of Odorants Modulate Their Association to Human Odorant Binding Protein

Biomolecules ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 145
Author(s):  
Tarsila G. Castro ◽  
Carla Silva ◽  
Teresa Matamá ◽  
Artur Cavaco-Paulo
Keyword(s):  
Molecular Weight ◽  
Medical Diagnosis ◽  
Binding Protein ◽  
Binding Energies ◽  
Odorant Binding Protein ◽  
Biotechnological Applications ◽  
In Silico Docking ◽  
Degree Of Unsaturation ◽  
Odorant Binding ◽  
Human Olfaction

The binding of known odorant molecules to the human odorant-binding protein (hOBP) was evaluated in silico. Docking experiments elucidate the preferable binding site and binding affinity of odorant molecules to hOBP. The physicochemical properties molecular weight (MW), vapor pressure (Vp), hydrophobicity level (logP), number of double bonds (NºDB), degree of unsaturation (DoU) and the chemical classification, were selected for the study of odorant modulation. Here, these properties were analyzed concerning 30 pleasant and 30 unpleasant odorants, chosen to represent a wide variety of compounds and to determine their influence on the binding energy to hOBP. Our findings indicate that MW, logP and Vp are the most important odorant variables, directly correlated to odorant-binding energies (ΔGbinding) towards hOBP. Understanding how the odorants behave when complexed with the OBP in human olfaction opens new possibilities for the development of future biotechnological applications, including sensory devices, medical diagnosis, among others.

scholarly journals Odorant-binding protein. Characterization of ligand binding.

1990 ◽  
Vol 265 (11) ◽  
pp. 6118-6125
Author(s):  
J Pevsner ◽  
V Hou ◽  
A M Snowman ◽  
S H Snyder
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Protein Characterization ◽  
Odorant Binding Protein ◽  
Odorant Binding

Molecular and Functional Characterization of One Odorant-Binding Protein Gene OBP3 in Bemisia tabaci (Hemiptera: Aleyrodidae)

2019 ◽  
Author(s):  
Ran Wang ◽  
Yuan Hu ◽  
Peiling Wei ◽  
Cheng Qu ◽  
Chen Luo
Keyword(s):  
Host Plant ◽  
Bemisia Tabaci ◽  
Binding Protein ◽  
Insect Pest ◽  
Critical Role ◽  
Functional Characterization ◽  
Odorant Binding Protein ◽  
Binding Characteristics ◽  
And Function ◽  
Odorant Binding

Abstract Odorant binding proteins (OBPs) of insects play a critical role in chemical perceptions and choice of insect host plant. Bemisia tabaci is a notorious insect pest which can damage more than 600 plant species. In order to explore functions of OBPs in B. tabaci, here we investigated binding characteristics and function of odorant-binding protein 3 in B. tabaci (BtabOBP3). The results indicated that BtabOBP3 shows highly similar sequence with OBPs of other insects, including the typical signature motif of six cysteines. The recombinant BtabOBP3 protein was obtained, and the evaluation of binding affinities to tested volatiles of host plant was conducted, then the results indicated that β-ionone had significantly higher binding to BtabOBP3 among other tested plant volatiles. Furthermore, silencing of BtabOBP3 significantly altered choice behavior of B. tabaci to β-ionone. In conclusion, it has been demonstrated that BtabOBP3 exerts function as one carrier of β-ionone and the results could be contributed to reveal the mechanisms of choosing host plant in B. tabaci.

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