Related Experiment Video
Updated: May 30, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
Published on: March 21, 2025
Colloidal properties of biodegradable nanoparticles influence interaction with amyloid-β peptide
Davide Brambilla1, Hayfa Souguir, Julien Nicolas
1Laboratoire de Physico-Chimie, Pharmacotechnie et Biopharmacie, Univ. Paris-Sud, Faculté de Pharmacie, 5 rue Jean-Baptiste Clément, Châtenay-Malabry cedex, France.
Abstract:
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by the extracellular deposition of amyloid-β peptides (Aβ). During the past few years, promising approaches based on nanotechnologies have emerged to alter Aβ aggregation and its related toxicity. This study aims to investigate the influence of the nanoparticle colloidal properties over the interaction with Aβ peptide 1-42 (Aβ(1-42)). Using capillary electrophoresis with laser-induced fluorescence detection, it was shown that biodegradable poly(ethylene glycol)-block-polylactide (PEG-b-PLA) nanoparticles were able to interact with Aβ(1-42) peptide leading to its uptake in rather short time periods. In addition, we highlighted the crucial role of the nanocarrier colloidal properties on the uptake kinetics. Whereas nanoparticles stabilized by sodium cholate (lower size and higher negative surface charge) gave optimum uptake kinetics, nanoparticles stabilized with others surfactants presented lower interactions. In contrast, PEG density seemed to have no influence on the interaction when sodium cholate was used for the preparation. This study intends to give new insights into Aβ(1-42) peptide interaction with nanoparticulate systems by helping to determine suitable nanoparticle characteristics regarding forthcoming therapeutic strategies against AD.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Colloidal precipitates

