scholarly journals Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster

2003 ◽  
Vol 10 (9) ◽  
pp. 694-700 ◽  
Author(s):  
Schoen W Kruse ◽  
Rui Zhao ◽  
Dean P Smith ◽  
David N M Jones
Keyword(s):  
Drosophila Melanogaster ◽  
Binding Site ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Odorant Binding

scholarly journals Natural Variation, Functional Pleiotropy and Transcriptional Contexts of Odorant Binding Protein Genes in Drosophila melanogaster

Genetics ◽  
2010 ◽  
Vol 186 (4) ◽  
pp. 1475-1485 ◽  
Author(s):  
Gunjan H. Arya ◽  
Allison L. Weber ◽  
Ping Wang ◽  
Michael M. Magwire ◽  
Yazmin L. Serrano Negron ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Natural Variation ◽  
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.

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