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ACS Nano. 2017 Feb 28;11(2):1328-1339. doi: 10.1021/acsnano.6b05992. Epub 2017 Jan 31.

Nanoparticles Associate with Intrinsically Disordered RNA-Binding Proteins.

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Department of Biochemistry, Erasmus Medical Center , Rotterdam 3015CE, The Netherlands.
Institute of Systematics and Ecology of Animals, SB RAS , Novosibirsk 630091, Russia.


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.


RNA-binding proteins; intrinsically disordered proteins; nanoparticles; proteomics; stress granules

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