TY - JOUR
T1 - New method based on capillary electrophoresis with laser-induced fluorescence detection (CE-LIF) to monitor interaction between nanoparticles and the amyloid-β peptide
AU - Brambilla, Davide
AU - Verpillot, Romain
AU - Taverna, Myriam
AU - De Kimpe, Line
AU - Le Droumaguet, Benjamin
AU - Nicolas, Julien
AU - Canovi, Mara
AU - Gobbi, Marco
AU - Mantegazza, Francesco
AU - Salmona, Mario
AU - Nicolas, Valérie
AU - Scheper, Wiep
AU - Couvreur, Patrick
AU - Andrieux, Karine
PY - 2010/12/15
Y1 - 2010/12/15
N2 - 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.
AB - 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.
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U2 - 10.1021/ac102045x
DO - 10.1021/ac102045x
M3 - Article
C2 - 21086977
AN - SCOPUS:78650336764
VL - 82
SP - 10083
EP - 10089
JO - Industrial And Engineering Chemistry Analytical Edition
JF - Industrial And Engineering Chemistry Analytical Edition
SN - 0003-2700
IS - 24
ER -