Current methods of protein analysis may be complex, expensive or burdensome, involving mass spectrometry or immunoassays. Many researchers analyse gene expression as a surrogate for proteins. A direct electrical method of protein analysis may provide benefits for researchers; costs are dependent on silicon scalability, workflow is likely to be simplified, and the information obtained through nanopore sensing is likely to be rich.
Oxford Nanopore is exploring the use of nanopores for the analysis of proteins by combining nanopores with ligands. A ligand is a molecule that can bind specifically to a site on a target protein. When used in the Oxford Nanopore technology platform, a bound ligand-protein construct may create characteristic disruption of a current running through a nanopore. It is desirable that this binding event should be reversible; the duration of a binding event provides further evidence of protein identity and the frequency of binding event provides information about concentration of that analyte.
The research below from Oxford Nanopore founder Professor Hagan Bayley's group illustrates the principal of this method, describing nanopore-ligand-protein interactions and the modification of a protein nanopore for the analysis of a protein kinase.
Stochastic detection of monovalent and bivalent protein-ligand interactions. Angew. Chem. Int. Ed. 43, 842-846 (2004)
Genetic modification of the protein pore to promote interaction with a protein analyte: Cheley, S., Xie, H. and Bayley, H. (2006) A genetically encoded pore for the stochastic detection of a protein kinase. Chembiochem. 7; 1923-1927
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