Speaker
Description
Surface Plasmon Resonance (SPR) provides a label-free optical platform for the detection of biomolecular interactions. While highly sensitive, its accuracy can be compromised by non-specific binding, which introduces background interference and obscures target-specific signals, particularly on probe-functionalized surfaces. To address this challenge, the present study systematically investigated the efficacy of bovine serum albumin (BSA) as a surface-blocking agent on probe-functionalized SPR sensor chips designed for the detection of multi-drug-resistant tuberculosis (MDR-TB)-associated genetic targets. The sensor surfaces were functionalized with thiolated DNA probes specific to MDR-TB mutations and subsequently exposed to varying concentrations of BSA (ranging from 0.02 to 0.8 mg/mL) to evaluate and optimize surface passivation and minimize non-specific adsorption. Controlled binding assays between the immobilized probes and complementary target sequences were performed and analyzed using a Kretschmann configuration SPR biosensing platform. This approach enabled a systematic assessment of the impact of BSA blocking on signal specificity, surface coverage, and overall biosensor performance. Analysis of the resonance angle shifts showed that BSA blocking reduced non-specific binding interactions and improved signal-to-noise ratios. These findings suggested that BSA can be an effective strategy for minimizing background noise in SPR-based assays for biomolecular detection.
| Apply for student award at which level: | None |
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| Consent on use of personal information: Abstract Submission | Yes, I ACCEPT |