High Speed AFM and NanoInfrared Spectroscopy Investigation of Aβ Peptide Variants and Their Interaction With POPC/SM/Chol/GM1 Model Membranes.

Due to an aging population, neurodegenerative diseases such as Alzheimer's disease (AD) have become a major health issue. In the case of AD, Aβ peptides have been identified as one of the markers of the disease with the formation of senile plaques via their aggregation, and could play a role in memory impairment and other tragic syndromes associated with the disease. Many studies have shown that not only the morphology and structure of Aβ peptide assembly are playing an important role in the formation of amyloid plaques, but also the interactions between Aβ and the cellular membrane are crucial regarding the aggregation processes and toxicity of the amyloid peptides.

Nanoparticles With a Specific Size and Surface Charge Promote Disruption of the Secondary Structure and Amyloid-Like Fibrillation of Human Insulin Under Physiological Conditions.

Nanoparticles attract much interest as fluorescent labels for diagnostic and therapeutic tools, although their applications are often hindered by size- and shape-dependent cytotoxicity. This cytotoxicity is related not only to the leak of toxic metals from nanoparticles into a biological solution, but also to molecular cytotoxicity effects determined by the formation of a protein corona, appearance of an altered protein conformation leading to exposure of cryptic epitopes and cooperative effects involved in the interaction of proteins and peptides with nanoparticles. In the last case, nanoparticles may serve, depending on their nature, as centers of self-association or fibrillation of proteins and peptides, provoking amyloid-like proteinopathies, or as inhibitors of self-association of proteins, or they can self-assemble on biopolymers as on templates.

Self-assembly properties and dynamics of synthetic proteo-nucleic building blocks in solution and on surfaces.

Synthetic proteo-nucleic structures (PDNAs) encompassing a single-stranded DNA sequence covalently attached to a redox protein domain able to interact with surface or matrix were designed and characterized. They constitute versatile building blocks alternative to regular DNA for creating scaffolds with optical, electrical, or catalytic properties. PDNAs self-assemble in the presence of complementary oligonucleotides, to form a network of protein domains linked by double-stranded DNA segments.