Hybrid pore formation by directed insertion of a-haemolysin into solid-state nanopores

UNCG Author/Contributor (non-UNCG co-authors, if there are any, appear on document)
Adam Hall, Assistant Professor (Creator)
The University of North Carolina at Greensboro (UNCG )
Web Site: http://library.uncg.edu/

Abstract: Most experiments on nanopores have concentrated on the pore-forming protein a-haemolysin (aHL) and on artificial pores in solid-state membranes. While biological pores offer an atomically precise structure and the potential for genetic engineering, solid-state nanopores offer durability, size and shape control, and are also better suited for integration into wafer-scale devices. However, each system has significant limitations: aHL is difficult to integrate because it relies on delicate lipid bilayers for mechanical support, and the fabrication of solid-state nanopores with precise dimensions remains challenging. Here we show that these limitations may be overcome by inserting a single aHL pore into a solid-state nanopore. A double-stranded DNA attached to the protein pore is threaded into a solid-state nanopore by electrophoretic translocation. Protein insertion is observed in 30–40% of our attempts, and translocation of single-stranded DNA demonstrates that the hybrid nanopore remains functional. The hybrid structure offers a platform to create wafer-scale device arrays for genomic analysis, including sequencing.

Additional Information

Nature Nanotechnology
Language: English
Date: 2010
Nanobiotechnology, Nanomedicine

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