Conformational properties of intrinsically disordered proteins bound to the surface of silica nanoparticles

Conclusions IDPs maintain structural disorder inside HC, experiencing minor, protein-specific, induced folding and stabilization against further conformational transitions, such as formation of intermolecular beta-sheets upon dehydration. The HC is formed by a single layer of protein molecules. SC likely plays a key role stabilizing amyloidogenic α-synuclein conformers. General significance Protein-NP interactions can mimic those with macromolecular partners, allowing dissection of contributing factors by rational design of NP surfaces. Application of NPs in vivo should be carefully tested for amyloidogenic potential. Graphical abstract
Source: Biochimica et Biophysica Acta (BBA) General Subjects - Category: Biochemistry Source Type: research