Study on Snake Venom Protein-Antibody Interaction by Surface Plasmon Resonance Spectroscopy

Study on Snake Venom Protein-Antibody Interaction by Surface Plasmon Resonance Spectroscopy

The development of a portable and inexpensive surface plasmon resonance (SPR) measurement device with the integrated biosensor for the detection of snake venom protein is presented in this paper. For the construction of the sensing element, amine coupling chemistry is used to bio-functionalize silve...

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Bibliographic Details
Published in:Photonic sensors (Berlin) Vol. 8; no. 3; pp. 193 - 202
Main Authors: Choudhury, Subhankar N., Konwar, Barlina, Kaur, Simran, Doley, Robin, Mondal, Biplob
Format: Journal Article
Language:English
Published: Singapore Springer Singapore 01-09-2018
Springer Nature B.V
SpringerOpen
Subjects:
Antibodies
biosensor
Biosensors
Buffer solutions
Buffers (chemistry)
Coupling (molecular)
Ethanol
Fourier transforms
Lasers
Measurement Science and Instrumentation
Microwaves
Molecular chains
Molecular interactions
Optical Devices
Optics
Organic chemistry
Photonics
Physics
Physics and Astronomy
Portable equipment
Proteins
Regular
RF and Optical Engineering
Snakes
Sodium chloride
Surface plasmon resonance
Venom
venom protein
venom protein
Surface plasmon resonance
biosensor
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Summary:The development of a portable and inexpensive surface plasmon resonance (SPR) measurement device with the integrated biosensor for the detection of snake venom protein is presented in this paper. For the construction of the sensing element, amine coupling chemistry is used to bio-functionalize silver coated glass slide with antibodies like immunoglobulin (IgG). The immobilization of the antibody is confirmed by spectroscopic measurements like ultraviolet-visible spectroscopy (UV-Vis) and Fourier-transforms infrared spectroscopy (FTIR). The device is calibrated with the standard solution of sodium chloride and ethanol before testing venom protein samples. To investigate the bio-molecular interactions, crude venom of Indian cobra (concentration range: 0.1 mg/ml‒1.0 mg/ml) in the phosphate buffer solution (PBS) are exposed to the biosensor. The experimentally measured data indicate the shift in the plasmon resonance angle from its initial value (52°) to 54° for 0.1 mg/ml and 60° for 1.0 mg/ml protein solution.
ISSN:1674-9251
2190-7439
DOI:10.1007/s13320-018-0501-1