Publications by authors named "J C Aude"
Unlabelled: Dual-fraction proteomics reveals a novel class of proteins impacted by nanoparticle exposure.
Background: Nanoparticles (NPs) interact with cellular proteomes, altering biological processes. Understanding these interactions requires comprehensive analyses beyond solely characterizing the NP corona.
The canonical BRG/BRM-associated factor (cBAF) complex is essential for chromatin opening at enhancers in mammalian cells. However, the nature of the open chromatin remains unclear. Here, we show that, in addition to producing histone-free DNA, cBAF generates stable hemisome-like subnucleosomal particles containing the four core histones associated with 50-80 bp of DNA.
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- Protein aggregation in biotherapeutics can diminish their effectiveness and cause harmful immune reactions, and the role of plastic materials in this process is not fully understood.
- The study investigates how different material surfaces (like polypropylene and glass) and mechanical agitation affect the stability of various proteins and finds that certain proteins are more vulnerable to destabilization under these conditions.
- The authors suggest that reducing any one of these stress factors—material type, air exposure, or agitation—can help preserve protein stability and mitigate adverse effects.
Protein adsorption on nanoparticles is an important field of study, particularly with regard to nanomedicine and nanotoxicology. Many factors can influence the composition and structure of the layer(s) of adsorbed proteins, the so-called protein corona. However, the role of protein size has not been specifically investigated, although some evidence has indicated its potential important role in corona composition and structure.
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- Biomolecules, especially proteins, form a "protein corona" on the surfaces of nanoparticles (NPs), influencing their biological behavior and toxicity.
- The study focused on silica nanoparticles (SiNPs) of various sizes and found that larger NPs tend to have more proteins adsorbed per surface area, although most proteins were similar across different NP sizes.
- Key factors driving protein adsorption include electrostatic interactions and disordered protein regions, while the polypeptide sequence length also plays a significant role, suggesting that curvature is not a primary factor in complex biological environments.