研究目的
To introduce a novel plasmonic approach to study the binding kinetics of protein-ligand interactions through the dimerization of functionalized silver nanoparticles (Ag NPs) by UV-Vis spectroscopy, serving as probes for antigen detection and quantification.
研究成果
The study successfully introduced a novel plasmonic approach to study protein interaction kinetics through the dimerization of functionalized Ag NPs. The method provides insights into the complex reaction mechanism of protein interactions and has potential applications in the development of SPR-based bioassays for antigen detection and quantification.
研究不足
The study is limited to the specific interaction between biotin and streptavidin and the formation of dimers of functionalized Ag NPs. The approach may require adaptation for studying other protein interactions.
1：Experimental Design and Method Selection:
The study involved the functionalization of Ag NPs with biotin-HPDP and streptavidin molecules, followed by the induction of dimer formation through the addition of gliadin-specific biotinylated IgG antibodies. The dimerization kinetics was monitored using UV-Vis spectroscopy.
2：Sample Selection and Data Sources:
Ag NPs of three different average diameters (36 nm, 46 nm, and 76 nm) were synthesized and functionalized. The kinetics was studied as a function of Ag NPs size and at different concentrations of IgG-Biot.
3：List of Experimental Equipment and Materials:
AgNO3, sodium citrate, EZ-Link Biotin-HPDP, streptavidin, biotinylated IgG antibody specific to wheat gliadin, phosphate buffer solution, polysorbate 20, diluent solution.
4：Experimental Procedures and Operational Workflow:
Ag NPs were synthesized, functionalized, and then mixed with IgG-Biot to induce dimerization. The process was monitored using UV-Vis spectroscopy, TEM, and DLS.
5：Data Analysis Methods:
The dimer concentration was determined from the extinction depletion using Mie theory. The kinetics data were modeled using Kintecus software to elucidate the reaction mechanism.
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