Odorant-Binding Proteins as Sensing Elements for Odour Monitoring

被引:82
作者
Pelosi, Paolo [1 ]
Zhu, Jiao [1 ]
Knoll, Wolfgang [1 ]
机构
[1] Austrian Inst Technol GmbH, Biosensor Technol, Konrad Lorenzstr 24, A-3430 Tulln, Austria
关键词
odorant-binding proteins; chemosensory proteins; Niemann-Pick C2 proteins; site-directed mutagenesis; biosensors; X-RAY STRUCTURE; PHEROMONE-BINDING; BOMBYX-MORI; LIGAND-BINDING; CHEMICAL COMMUNICATION; OLFACTORY BIOSENSOR; CRYSTAL-STRUCTURE; SOLUBLE-PROTEINS; SCHISTOCERCA-GREGARIA; INFRARED-SPECTROSCOPY;
D O I
10.3390/s18103248
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
Odour perception has been the object of fast growing research interest in the last three decades. Parallel to the study of the corresponding biological systems, attempts are being made to model the olfactory system with electronic devices. Such projects range from the fabrication of individual sensors, tuned to specific chemicals of interest, to the design of multipurpose smell detectors using arrays of sensors assembled in a sort of artificial nose. Recently, proteins have attracted increasing interest as sensing elements. In particular, soluble olfaction proteins, including odorant-binding proteins (OBPs) of vertebrates and insects, chemosensory proteins (CSPs) and Niemann-Pick type C2 (NPC2) proteins possess interesting characteristics for their use in sensing devices for odours. In fact, thanks to their compact structure, their soluble nature and small size, they are extremely stable to high temperature, refractory to proteolysis and resistant to organic solvents. Moreover, thanks to the availability of many structures solved both as apo-proteins and in complexes with some ligands, it is feasible to design mutants by replacing residues in the binding sites with the aim of synthesising proteins with better selectivity and improved physical properties, as demonstrated in a number of cases.
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页数:19
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