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Issue 32, 2017
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SDS-assisted protein transport through solid-state nanopores

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Abstract

Using nanopores for single-molecule sequencing of proteins – similar to nanopore-based sequencing of DNA – faces multiple challenges, including unfolding of the complex tertiary structure of the proteins and enforcing their unidirectional translocation through nanopores. Here, we combine molecular dynamics (MD) simulations with single-molecule experiments to investigate the utility of SDS (Sodium Dodecyl Sulfate) to unfold proteins for solid-state nanopore translocation, while simultaneously endowing them with a stronger electrical charge. Our simulations and experiments prove that SDS-treated proteins show a considerable loss of the protein structure during the nanopore translocation. Moreover, SDS-treated proteins translocate through the nanopore in the direction prescribed by the electrophoretic force due to the negative charge impaired by SDS. In summary, our results suggest that SDS causes protein unfolding while facilitating protein translocation in the direction of the electrophoretic force; both characteristics being advantageous for future protein sequencing applications using solid-state nanopores.

Graphical abstract: SDS-assisted protein transport through solid-state nanopores

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Publication details

The article was received on 06 Apr 2017, accepted on 08 Jul 2017 and first published on 12 Jul 2017


Article type: Paper
DOI: 10.1039/C7NR02450A
Citation: Nanoscale, 2017,9, 11685-11693
  • Open access: Creative Commons BY-NC license
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    SDS-assisted protein transport through solid-state nanopores

    L. Restrepo-Pérez, S. John, A. Aksimentiev, C. Joo and C. Dekker, Nanoscale, 2017, 9, 11685
    DOI: 10.1039/C7NR02450A

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