Nanoparticles are capable of penetrating cells, but little is known about the way they interact with intracellular proteome. Here we show that inorganic nanoparticles associate with low-complexity, intrinsically disordered proteins from HeLa cytosolic protein extracts in nondenaturing in vitro nanoparticle pull-down assays. Intrinsic protein disorder associates with structural mobility, suggesting that side-chain flexibility plays an important role in the driving of a protein to nanoparticle absorption. Disordered protein domains are often found in a diverse group of RNA-binding proteins. Consequently, the nanoparticle-associated proteomes were enriched in subunits of RNA-processing protein complexes. In turn, this indicates that within a cell, nanoparticles might interfere with protein synthesis triggering a range of cellular responses.

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Keywords intrinsically disordered proteins, nanoparticles, proteomics, RNA-binding proteins, stress granules
Persistent URL dx.doi.org/10.1021/acsnano.6b05992, hdl.handle.net/1765/98398
Journal ACS Nano
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Citation
Romashchenko, A.V, Kan, T.W, Petrovski, D.V, Gerlinskaya, L.A, Moshkin, M.P, & Moshkin, Y.M. (2017). Nanoparticles Associate with Intrinsically Disordered RNA-Binding Proteins. ACS Nano, 11(2), 1328–1339. doi:10.1021/acsnano.6b05992