Abstract
AbstractIn the serum sample of swine flu patients, the novel Serum Amyloid A (SAA) protein has been secreted in higher concentration (49.4±14.1 μg mL−1) with respect tothe normal subject (12.2±15.0 μg mL−1), so SAA protein has been used in swine flu diagnosis. In present work, we developed nanostructured mesoporous carbon (mPC) based electrochemical biosensor for the swine flu detection. The mPC was synthesized through the thermal decomposition process, and with 3‐aminopropyltriethoxy silane (APTES), amine functionalization of mPC was carried out. The obtained product was further deposited onto the functionalized indium tin oxide (ITO) coated glass electrode using electrophoretic deposition unit with 40V DC voltage for 150 sec. Next, biofunctionalization with monoclonal anti‐SAA antibodies (anti‐SAA) was carried out onto the APTES/mPC/ITO electrode by EDC‐NHS covalent chemistry and bovine serum albumin (BSA) was used to block non‐specific binding sites. The structural and morphological, characterization of the mPC and fabricated electrodes were investigated using X‐ray diffraction, Raman spectroscopy, scanning electron microscopy, transmission electron microscopy, atomic force microscopy, and Fourier‐transform infrared spectroscopy. However, surface area and porosity analysis were investigated via Brauner‐Emmett‐Teller technique. Next, the electrochemical characterization and response studies were performed by cyclic voltammetry technique. The fabricated biosensing platform (BSA/anti‐SAA/APTES/mPC/ITO) exhibited excellent sensitivity of 1.69 μA mL μg−1 cm−2, wider linear detection range between 30–70 μg mL−1 with a limit of detection of 3.1 μg mL−1. The biosensing performance of the fabricated biosensing platform was also investigated in artificial serum samples and showed a good correlation with the obtained electrochemical response.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.