Surface Plasmon Resonance Detection For Drug / Protein Interactions And Dna Amplification

In this paper we reviewed the development of SPR biosensor. We also reviewed the main applications of SPR biosensors using examples from a variety of biological systems. SPR biosensors can measure the interactions of biomolecules directly without the need for labeling. This feature has allowed these analytical instruments to become a central tool for characterizing and quantifying biomolecular interactions. Due to the fast response and high sensitivity of SPR-based biosensors compared to other technologies such as enzyme or radiolabeling methods, biosensors can be used to study a large variety of biomolecular mechanisms, ranging from protein/protein, antibody/antigen, and receptor/ligand interactions to the characterization of even low molecular weight compounds. The BI 1000 SPR instrument combined with a flow injection (FI) device was used for the interaction between drug and protein, and also for the new system of analyzing DNA sequence amplifiedly.Through a "layer-by-layer" way, the 11-mercaptoundecanoic acid (MUA) was immobilized on the gold-covered glass to form a MUA monolayer, By carbodiimide methods (NHS/EDC), the MUA was activated and BSA was coupled to the carboxylic groups on the surface. The unreacted sites on the surface were blocked by Amino-ethanol-HCl (AE). Then drug Diclofenac Sodium (DFS) was injected to flow over the BSA sensor. When the interaction happened, the signal of SPR changed. The work discussed a series of SPR sensorgrams corresponding to the DFS of different concentrations. The signal presented good linear relation to the concentrations between 50 to 300μmol/L, which demonstrated that the specific interaction has occured. It provides certain signification abstractly to study the characteristic of drugs. Because of the protein sensor, we can utilize the model to investigate the interactions between the protein and other drugs.Hybridization of the deoxyribonucleic acid (DNA) target followed by the association of the biotin-tagged detection probes yields a "sandwich" (a three-component double-stranded) assembly. The enzyme can be modified on the DNA duplexes-covered surface via interaction of the biotin tags with the streptavidin-HRP conjugates (SA-HRP). The HRP-biocatalyzed oxidation of 4-chloro-l-naphthol (CN) in the presence of H₂O₂ and the subsequent precipitation of benzo-chloro-hexadienone covered on the multilayers. Because of the insoluble product, the SPR signal was amplified dramatically to arrive at an adequately low detection-limit. The method is shown to be reproducible and to possess high sequence specificity. ODN target concentration as low as 10 fmol/L can be measured using the present method.