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1.D.132.  The Synthetic DNA/alpha-Hemolysin Pore (DNA-HL) Family

Henning-Knechtel et al. 2017 have developed a novel approach for creating membrane-spanning protein-based pores. The construction principle is based on using well-defined, circular DNA nanostructures to arrange a precise number of pore-forming protein toxin monomers. Protein pores are constructed with specifically set diameters with artificial alpha-hemolysin (αHL) pores. The DNA/αHL hybrid nanopores are composed of twelve, twenty or twenty-six monomers and show stable insertion into lipid bilayers. Electrical recordings and steady pore size-dependent current levels can be obtained. This approach successfully advances the applicability of nanopores, in particular towards label-free studies of single molecules in large nanoscaled biological structures (Henning-Knechtel et al. 2017).

References associated with 1.D.132 family:

Henning-Knechtel, A., J. Knechtel, and M. Magzoub. (2017). DNA-assisted oligomerization of pore-forming toxin monomers into precisely-controlled protein channels. Nucleic Acids Res 45: 12057-12068. 29088457