Prediction of the key binding site of odorant-binding protein ofHolotrichia oblita Faldermann (Coleoptera: Scarabaeida)

2014 ◽  
pp. n/a-n/a ◽  
Author(s):  
X. Zhuang ◽  
Q. Wang ◽  
B. Wang ◽  
T. Zhong ◽  
Y. Cao ◽  
...  
Keyword(s):  
Binding Site ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Odorant Binding

scholarly journals The Crystal Structure of Odorant Binding Protein 7 from Anopheles gambiae Exhibits an Outstanding Adaptability of Its Binding Site

2011 ◽  
Vol 414 (3) ◽  
pp. 401-412 ◽  
Author(s):  
Amandine Lagarde ◽  
Silvia Spinelli ◽  
Mariella Tegoni ◽  
Xiaoli He ◽  
Lin Field ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Anopheles Gambiae ◽  
Binding Site ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Odorant Binding

scholarly journals A Highly Selective Biosensor Based on Peptide Directly Derived from the HarmOBP7 Aldehyde Binding Site

Sensors ◽  
2019 ◽  
Vol 19 (19) ◽  
pp. 4284 ◽  
Author(s):  
Tomasz Wasilewski ◽  
Bartosz Szulczyński ◽  
Marek Wojciechowski ◽  
Wojciech Kamysz ◽  
Jacek Gębicki
Keyword(s):  
Binding Site ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Experimental Results ◽  
Ligand Docking ◽  
Peptide Ligand ◽  
Optimal Length ◽  
Ligand Interaction ◽  
Chain Lengths ◽  
Odorant Binding

This paper presents the results of research on determining the optimal length of a peptide chain to effectively bind octanal molecules. Peptides that map the aldehyde binding site in HarmOBP7 were immobilized on piezoelectric transducers. Based on computational studies, four Odorant Binding Protein-derived Peptides (OBPPs) with different sequences were selected. Molecular modelling results of ligand docking with selected peptides were correlated with experimental results. The use of low-molecular synthetic peptides, instead of the whole protein, enabled the construction OBPPs-based biosensors. This work aims at developing a biomimetic piezoelectric OBPPs sensor for selective detection of octanal. Moreover, the research is concerned with the ligand binding affinity depending on different peptides’ chain lengths. The authors believe that the chain length can have a substantial influence on the type and effectiveness of peptide–ligand interaction. A confirmation of in silico investigation results is the correlation with the experimental results, which shows that the highest affinity to octanal is exhibited by the longest peptide (OBPP4 – KLLFDSLTDLKKKMSEC-NH2). We hypothesized that the binding of long chain aldehydes to the peptide, mimicking the binding site of HarmOBP7, induced a conformational change in the peptide deposited on a selected transducer. The constructed OBPP4-based biosensors were able to selectively bind octanal in the gas phase. It was also shown that the sensors were characterized by high selectivity with respect to octanal, as well as to acetaldehyde and benzaldehyde. The results indicate that the OBPP4 peptide, mimicking the binding domain in the Odorant Binding Protein, can provide new opportunities for the development of biomimicking materials in the field of odor biosensors.

scholarly journals In Silico Site-Directed Mutagenesis of the Anopheles gambiae Odorant Binding Protein 20

2016 ◽  
Vol 15 (2) ◽  
pp. 156-165
Author(s):  
Jose Isagani B. Janairo ◽  
Patricia Isabel K. Bravo ◽  
Ninna Louise G. Morano ◽  
Derrick Ethelbhert C. Yu
Keyword(s):  
Anopheles Gambiae ◽  
Binding Site ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Ligand Interaction ◽  
Host Seeking ◽  
Seeking Behavior ◽  
Odorant Binding

Abstract The Anopheles gambiae is a highly anthropophilic mosquito which is the leading vector for malaria. This disease has affected more than 500 million people worldwide. The Anopheles gambiae targets its hosts through the odors of the human skin and sweat where odorant molecules radiate. These odors elicit specific responses from the insect through the odorant – binding proteins (OBP). Recently, a specific type of OBP has been characterized which is known as the Anopheles gambiae odorant – binding protein 20 (AgamOBP20). This OBP is highly expressed in the female mosquito antennae during the peak of its host – seeking behavior and thus may play a role in olfactory perception. The binding site of the AgamOBP20 is composed primarily of hydrophobic residues wherein the importance of each residue is herein analysed to further understand the properties of AgamOBP20. This was carried out through computer – aided site – directed mutagenesis coupled with homology modelling and docking simulations wherein each residue in the binding site was changed to alanine and serine. Probable key amino acid residues were identified as LEU106, LEU107, and MET53 which are hypothesized to play a significant role in the protein – ligand interaction. These residues had the greatest impact in the binding free energy when mutated with alanine and serine. The presented results suggest that steric hindrance and hydrophobic interaction are crucial factors to consider on the manner in which the ligand binds with AgamOBP20. The molecular features and parameters obtained may be utilized for the development of new pesticides and repellents that are able to block the function of AgamOBP20 and may result to the disarray of the host – seeking behavior of the Anopheles gambiae.

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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