Dynamics of completely unfolded and native proteins through solid-state nanopores as a function of electric driving force

ACS Nano. 2011 May 24;5(5):3628-38. doi: 10.1021/nn1034795. Epub 2011 Apr 26.

Abstract

We report experimentally the dynamic properties of the entry and transport of unfolded and native proteins through a solid-state nanopore as a function of applied voltage, and we discuss the experimental data obtained as compared to theory. We show an exponential increase in the event frequency of current blockades and an exponential decrease in transport times as a function of the electric driving force. The normalized current blockage ratio remains constant or decreases for folded or unfolded proteins, respectively, as a function of the transmembrane potential. The unfolded protein is stretched under the electric driving force. The dwell time of native compact proteins in the pore is almost 1 order of magnitude longer than that of unfolded proteins, and the event frequency for both protein conformations is low. We discuss the possible phenomena hindering the transport of proteins through the pores, which could explain these anomalous dynamics, in particular, electro-osmotic counterflow and protein adsorption on the nanopore wall.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computer Simulation
  • Electromagnetic Fields
  • Electroporation / methods*
  • Models, Chemical*
  • Nanostructures / chemistry*
  • Nanostructures / radiation effects*
  • Nanostructures / ultrastructure
  • Porosity / radiation effects
  • Protein Unfolding
  • Proteins / chemistry*
  • Proteins / radiation effects*
  • Radiation Dosage
  • Stress, Mechanical

Substances

  • Proteins