Influence of Nanoparticle Size and Shape on Oligomer Formation of an Amyloidogenic Peptide.

ABSTRACT: Understanding the influence of macromolecular crowding and nanoparticles on the formation of in-register β-sheets, the primary structural component of amyloid fibrils, is a first step towards describing in vivo protein aggregation and interactions between synthetic materials and proteins. Using all atom molecular simulations in implicit solvent we illustrate the effects of nanoparticle size, shape, and volume fraction on oligomer formation of an amyloidogenic peptide from the transthyretin protein. Surprisingly, we find that inert spherical crowding particles destabilize in-register β-sheets formed by dimers while stabilizing β-sheets comprised of trimers and tetramers. As the radius of the nanoparticle increases crowding effects decrease, implying smaller crowding particles have the large

SUBMITTER: O'Brien EP 

PROVIDER: S-EPMC3117580 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature