Enhanced translocation of single DNA molecules through alpha-hemolysin nanopores by manipulation of internal charge

Proc Natl Acad Sci U S A. 2008 Dec 16;105(50):19720-5. doi: 10.1073/pnas.0808296105. Epub 2008 Dec 5.

Abstract

Both protein and solid-state nanopores are under intense investigation for the analysis of nucleic acids. A crucial advantage of protein nanopores is that site-directed mutagenesis permits precise tuning of their properties. Here, by augmenting the internal positive charge within the alpha-hemolysin pore and varying its distribution, we increase the frequency of translocation of a 92-nt single-stranded DNA through the pore at +120 mV by approximately 10-fold over the wild-type protein and dramatically lower the voltage threshold at which translocation occurs, e.g., by 50 mV for 1 event.s(-1).muM(-1). Further, events in which DNA enters the pore, but is not immediately translocated, are almost eliminated. These experiments provide a basis for improved nucleic acid analysis with protein nanopores, which might be translated to solid-state nanopores by using chemical surface modification.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Toxins / chemistry*
  • Bacterial Toxins / genetics
  • Biological Transport
  • DNA, Single-Stranded / chemistry*
  • Genetic Engineering
  • Hemolysin Proteins / chemistry*
  • Hemolysin Proteins / genetics
  • Nanostructures / chemistry*
  • Nanotechnology*
  • Point Mutation
  • Porosity
  • Protein Folding
  • Surface Properties

Substances

  • Bacterial Toxins
  • DNA, Single-Stranded
  • Hemolysin Proteins
  • staphylococcal alpha-toxin