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

• Published in: Photonic sensors (Berlin) 2018-09, Vol.8 (3), p.193-202
• Main Authors: Choudhury, Subhankar N., Konwar, Barlina, Kaur, Simran, Doley, Robin, Mondal, Biplob
• Format: Article
• Language: English
• 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
• ISSN: 1674-9251; 2190-7439
• DOI: 10.1007/s13320-018-0501-1

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.