Highly sensitive olfactory biosensors for the detection of volatile organic compounds by surface plasmon resonance imaging

Nowadays, monitoring of volatile organic compounds (VOCs) is very important in various domains. In this work, we aimed to develop sensitive olfactory biosensors using odorant binding proteins (OBPs) as sensing materials. Three rat OBP3 derivatives with customized binding properties were designed and...

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Published inBiosensors & bioelectronics Vol. 123; pp. 230 - 236
Main Authors Hurot, Charlotte, Brenet, Sophie, Buhot, Arnaud, Barou, Emilie, Belloir, Christine, Briand, Loïc, Hou, Yanxia
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 01.01.2019
Elsevier
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Abstract Nowadays, monitoring of volatile organic compounds (VOCs) is very important in various domains. In this work, we aimed to develop sensitive olfactory biosensors using odorant binding proteins (OBPs) as sensing materials. Three rat OBP3 derivatives with customized binding properties were designed and immobilized on the same chip for the detection of VOCs in solution by surface plasmon resonance imaging (SPRi). We demonstrated that the proteins kept their binding properties after the immobilization under optimized conditions. The obtained olfactory biosensors exhibited very low limits of detection in both concentration (200 pM of β-ionone) and in molecular weight of VOCs (100 g/mol for hexanal). Such a performance obtained with SPRi in solution is especially remarkable. We hypothesized that the binding of VOCs to the active sites of OBPs induced a local conformational change in the proteins. This change would give rise to a variation of refractive index, to which SPRi is extremely sensitive. In addition, the olfactory biosensors showed a high selectivity especially at relatively low VOC concentrations. With optimized regeneration procedures, they also showed very good repeatability not only from measurement to measurement but also from chip to chip with a lifespan up to almost two months. These olfactory biosensors are particularly interesting for trace detection of VOCs in solution. •Custom-made odorant binding proteins (OBPs) are used for olfactory biosensor development.•SPRi is efficient for the detection of volatile organic compounds in solution.•A local conformational change in OBPs has most likely amplified the optical signal.•The olfactory biosensors are highly sensitive and selective at low concentrations.
AbstractList Nowadays, monitoring of volatile organic compounds (VOCs) is very important in various domains. In this work, we aimed to develop sensitive olfactory biosensors using odorant binding proteins (OBPs) as sensing materials. Three rat OBP3 derivatives with customized binding properties were designed and immobilized on the same chip for the detection of VOCs in solution by surface plasmon resonance imaging (SPRi). We demonstrated that the proteins kept their binding properties after the immobilization under optimized conditions. The obtained olfactory biosensors exhibited very low limits of detection in both concentration (200 pM of β-ionone) and in molecular weight of VOCs (100 g/mol for hexanal). Such a performance obtained with SPRi in solution is especially remarkable. We hypothesized that the binding of VOCs to the active sites of OBPs induced a local conformational change in the proteins. This change would give rise to a variation of refractive index, to which SPRi is extremely sensitive. In addition, the olfactory biosensors showed a high selectivity especially at relatively low VOC concentrations. With optimized regeneration procedures, they also showed very good repeatability not only from measurement to measurement but also from chip to chip with a lifespan up to almost two months. These olfactory biosensors are particularly interesting for trace detection of VOCs in solution. •Custom-made odorant binding proteins (OBPs) are used for olfactory biosensor development.•SPRi is efficient for the detection of volatile organic compounds in solution.•A local conformational change in OBPs has most likely amplified the optical signal.•The olfactory biosensors are highly sensitive and selective at low concentrations.
Nowadays, monitoring of volatile organic compounds (VOCs) is very important in various domains. In this work, we aimed to develop sensitive olfactory biosensors using odorant binding proteins (OBPs) as sensing materials. Three rat OBP3 derivatives with customized binding properties were designed and immobilized on the same chip for the detection of VOCs in solution by surface plasmon resonance imaging (SPRi). We demonstrated that the proteins kept their binding properties after the immobilization under optimized conditions. The obtained olfactory biosensors exhibited very low limits of detection in both concentration (200 pM of β-ionone) and in molecular weight of VOCs (100 g/mol for hexanal). Such a performance obtained with SPRi in solution is especially remarkable. We hypothesized that the binding of VOCs to the active sites of OBPs induced a local conformational change in the proteins. This change would give rise to a variation of refractive index, to which SPRi is extremely sensitive. In addition, the olfactory biosensors showed a high selectivity especially at relatively low VOC concentrations. With optimized regeneration procedures, they also showed very good repeatability not only from measurement to measurement but also from chip to chip with a lifespan up to almost two months. These olfactory biosensors are particularly interesting for trace detection of VOCs in solution.
Nowadays, monitoring of volatile organic compounds (VOCs) is very important in various domains. In this work, we aimed to develop sensitive olfactory biosensors using odorant binding proteins (OBPs) as sensing materials. Three rat OBP3 derivatives with customized binding properties were designed and immobilized on the same chip for the detection of VOCs in solution by surface plasmon resonance imaging (SPRi). We demonstrated that the proteins kept their binding properties after the immobilization under optimized conditions. The obtained olfactory biosensors exhibited very low limits of detection in both concentration (200pM of beta-ionone) and in molecular weight of VOCs (100g/mol for hexanal). Such a performance obtained with SPRi in solution is especially remarkable. We hypothesized that the binding of VOCs to the active sites of OBPs induced a local conformational change in the proteins. This change would give rise to a variation of refractive index, to which SPRi is extremely sensitive. In addition, the olfactory biosensors showed a high selectivity especially at relatively low VOC concentrations. With optimized regeneration procedures, they also showed very good repeatability not only from measurement to measurement but also from chip to chip with a lifespan up to almost two months. These olfactory biosensors are particularly interesting for trace detection of VOCs in solution.
Author Hurot, Charlotte
Brenet, Sophie
Belloir, Christine
Briand, Loïc
Buhot, Arnaud
Hou, Yanxia
Barou, Emilie
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Keywords Odorant binding proteins
Volatile organic compound
Surface plasmon resonance imaging
Olfactory biosensor
odorant binding proteins
volatile organic compound
surface plasmon resonance imaging
ofactory biosensor
Language English
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Snippet Nowadays, monitoring of volatile organic compounds (VOCs) is very important in various domains. In this work, we aimed to develop sensitive olfactory...
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SubjectTerms Animals
Biosensing Techniques
Biotechnology
Engineering Sciences
Life Sciences
Odorant binding proteins
Olfactory biosensor
Rats
Receptors, Odorant - chemistry
Smell
Surface Plasmon Resonance
Surface plasmon resonance imaging
Volatile organic compound
Volatile Organic Compounds - chemistry
Volatile Organic Compounds - isolation & purification
Title Highly sensitive olfactory biosensors for the detection of volatile organic compounds by surface plasmon resonance imaging
URI https://dx.doi.org/10.1016/j.bios.2018.08.072
https://www.ncbi.nlm.nih.gov/pubmed/30201334
https://search.proquest.com/docview/2102338841
https://hal.science/hal-01915890
Volume 123
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