New Method Based on Capillary Electrophoresis with Laser-Induced Fluorescence Detection (CE-LIF) to Monitor Interaction between Nanoparticles and the Amyloid-β Peptide

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• 作者：Davide Brambilla ; Romain Verpillot ; Myriam Taverna ; Line De Kimpe ; Benjamin Le Droumaguet ; Julien Nicolas ; Mara Canovi ; Marco Gobbi ; Francesco Mantegazza ; Mario Salmona ; Valrie Nicolas ; Wiep Scheper
• 刊名：Analytical Chemistry
• 出版年：2010
• 出版时间：December 15, 2010
• 年：2010
• 卷：82
• 期：24
• 页码：10083-10089
• 全文大小：296K
• 年卷期：v.82,no.24(December 15, 2010)
• ISSN：1520-6882

文摘

A novel application of capillary electrophoresis with laser-induced fluorescence detection (CE-LIF) was proposed to efficiently detect and monitor the interaction between polymeric nanoparticles and the β-Amyloid peptide (Aβ₁₋₄₂), a biomarker for Alzheimer’s Disease (AD), at concentrations close to physiological conditions. The CE-LIF method allowed the interaction between PEGylated poly(alkyl cyanoacrylate) nanoparticles (NPs) and the soluble Aβ₁₋₄₂ peptide monomers to be highlighted. These results were confirmed by surface plasmon resonance (SPR) and confocal laser scanning microscopy (CLSM). Whereas SPR showed an interaction between the NPs and the Aβ₁₋₄₂ peptide, CLSM allowed the formation of large aggregates/assemblies at high NP and peptide concentrations to be visualized. All these results suggested that these nanoparticles could bind the Aβ₁₋₄₂ peptide and influence its aggregation kinetics. Interestingly, the non-PEGylated poly(alkyl cyanoacrylate) NPs did not alter the aggregation kinetics of the Aβ₁₋₄₂ peptide, thus emphasizing the high level of discrimination of the CE-LIF method with respect to NPs.