Please use this identifier to cite or link to this item: http://localhost/handle/Hannan/598198
Title: Surface plasmon resonance immunoassay for cortisol determination with a self-assembling denaturalised bovine serum albumin layer on surface plasmon resonance chip
Authors: Xing Chen;Lulu Zhang;Dafu Cui
subject: molecule determination|atomic force microscopy technology|antibody concentration|immune reaction|cortisol antibody|denaturalised bovine serum albumin layer self-assembly|chip surface morphology|dBSA-SPR-chip|cortisol determination|cortisol derivative|surface plasmon resonance immunoassay|dextran-SPR-chip|surface plasmon resonance chip|surface modification method
Year: 2016
Publisher: IEEE
Abstract: A surface modification method has been developed to fabricate surface plasmon resonance (SPR) chip for small molecule determination. A novel denaturalised bovine serum albumin (dBSA)-SPR-chip was fabricated by a self-assembling method, while a dextran-SPR-chip was prepared by using a traditional method. The surface morphologies of the two chips were investigated by atomic force microscopy technology and their optical properties were characterised by using our home-made SPR analytical instrument. The surface binding capacity of the dBSA-SPR-chip is 2.5 times higher than that of the dextran-SPR-chip. On the basis of the experiments of immune reactions between cortisol antibody and cortisol derivative, the sensitivity of the dBSA-SPR-chip is much higher than that of the dextran-SPR-based SPR-chip. The antibody concentration was optimised at about 10 μg/ml in order to obtain high sensitivity, which was used in the followed inhibition immunoassays. The lowest detection limit for cortisol is 1 ng/ml with a linear range of 5-100 ng/ml by using the dBSA-SPR-chip. These dBSA-SPR-chips can also be applied to detect other small molecules based on the indirect inhibitive immunoassay.
Description: 
URI: http://localhost/handle/Hannan/185469
http://localhost/handle/Hannan/598198
ISSN: 1750-0443
volume: 11
issue: 1
Appears in Collections:2016

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Title: Surface plasmon resonance immunoassay for cortisol determination with a self-assembling denaturalised bovine serum albumin layer on surface plasmon resonance chip
Authors: Xing Chen;Lulu Zhang;Dafu Cui
subject: molecule determination|atomic force microscopy technology|antibody concentration|immune reaction|cortisol antibody|denaturalised bovine serum albumin layer self-assembly|chip surface morphology|dBSA-SPR-chip|cortisol determination|cortisol derivative|surface plasmon resonance immunoassay|dextran-SPR-chip|surface plasmon resonance chip|surface modification method
Year: 2016
Publisher: IEEE
Abstract: A surface modification method has been developed to fabricate surface plasmon resonance (SPR) chip for small molecule determination. A novel denaturalised bovine serum albumin (dBSA)-SPR-chip was fabricated by a self-assembling method, while a dextran-SPR-chip was prepared by using a traditional method. The surface morphologies of the two chips were investigated by atomic force microscopy technology and their optical properties were characterised by using our home-made SPR analytical instrument. The surface binding capacity of the dBSA-SPR-chip is 2.5 times higher than that of the dextran-SPR-chip. On the basis of the experiments of immune reactions between cortisol antibody and cortisol derivative, the sensitivity of the dBSA-SPR-chip is much higher than that of the dextran-SPR-based SPR-chip. The antibody concentration was optimised at about 10 μg/ml in order to obtain high sensitivity, which was used in the followed inhibition immunoassays. The lowest detection limit for cortisol is 1 ng/ml with a linear range of 5-100 ng/ml by using the dBSA-SPR-chip. These dBSA-SPR-chips can also be applied to detect other small molecules based on the indirect inhibitive immunoassay.
Description: 
URI: http://localhost/handle/Hannan/185469
http://localhost/handle/Hannan/598198
ISSN: 1750-0443
volume: 11
issue: 1
Appears in Collections:2016

Files in This Item:
File Description SizeFormat 
7393900.pdf263.65 kBAdobe PDFThumbnail
Preview File
Title: Surface plasmon resonance immunoassay for cortisol determination with a self-assembling denaturalised bovine serum albumin layer on surface plasmon resonance chip
Authors: Xing Chen;Lulu Zhang;Dafu Cui
subject: molecule determination|atomic force microscopy technology|antibody concentration|immune reaction|cortisol antibody|denaturalised bovine serum albumin layer self-assembly|chip surface morphology|dBSA-SPR-chip|cortisol determination|cortisol derivative|surface plasmon resonance immunoassay|dextran-SPR-chip|surface plasmon resonance chip|surface modification method
Year: 2016
Publisher: IEEE
Abstract: A surface modification method has been developed to fabricate surface plasmon resonance (SPR) chip for small molecule determination. A novel denaturalised bovine serum albumin (dBSA)-SPR-chip was fabricated by a self-assembling method, while a dextran-SPR-chip was prepared by using a traditional method. The surface morphologies of the two chips were investigated by atomic force microscopy technology and their optical properties were characterised by using our home-made SPR analytical instrument. The surface binding capacity of the dBSA-SPR-chip is 2.5 times higher than that of the dextran-SPR-chip. On the basis of the experiments of immune reactions between cortisol antibody and cortisol derivative, the sensitivity of the dBSA-SPR-chip is much higher than that of the dextran-SPR-based SPR-chip. The antibody concentration was optimised at about 10 μg/ml in order to obtain high sensitivity, which was used in the followed inhibition immunoassays. The lowest detection limit for cortisol is 1 ng/ml with a linear range of 5-100 ng/ml by using the dBSA-SPR-chip. These dBSA-SPR-chips can also be applied to detect other small molecules based on the indirect inhibitive immunoassay.
Description: 
URI: http://localhost/handle/Hannan/185469
http://localhost/handle/Hannan/598198
ISSN: 1750-0443
volume: 11
issue: 1
Appears in Collections:2016

Files in This Item:
File Description SizeFormat 
7393900.pdf263.65 kBAdobe PDFThumbnail
Preview File