Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores
Abstract
Engineered protein pores have several potential applications in biotechnology: as sensor elements in stochastic detection and ultrarapid DNA sequencing, as nanoreactors to observe single-molecule chemistry, and in the construction of nano- and micro-devices. One important class of pores contains molecular adapters, which provide internal binding sites for small molecules. Mutants of the α-hemolysin (αHL) pore that bind the adapter β-cyclodextrin (βCD) ∼104 times more tightly than the wild type have been obtained. We now use single-channel electrical recording, protein engineering including unnatural amino acid mutagenesis, and high-resolution x-ray crystallography to provide definitive structural information on these engineered protein nanopores in unparalleled detail.
- Publication:
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Proceedings of the National Academy of Science
- Pub Date:
- May 2010
- DOI:
- 10.1073/pnas.0914229107
- Bibcode:
- 2010PNAS..107.8165B