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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doi.org/10.1021/acsnano.6b05992, hdl.handle.net/1765/98398
ACS Nano
Department of Biochemistry

Romashchenko, A. V., Kan, T. W., Petrovski, D. V., Gerlinskaya, L. A., Moshkin, M. P., & Moshkin, Y. (2017). Nanoparticles Associate with Intrinsically Disordered RNA-Binding Proteins. ACS Nano, 11(2), 1328–1339. doi:10.1021/acsnano.6b05992