Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores

Arijit Banerjee, Ellina Mikhailova, Stephen Cheley, Li Qun Gu, Michelle Montoya, Yasuo Nagaoka, Eric Gouaux, Hagan Bayley

Research output: Contribution to journalArticle

76 Scopus citations

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 microdevices. 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.

Original languageEnglish (US)
Pages (from-to)8165-8170
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume107
Issue number18
DOIs
StatePublished - May 4 2010

Keywords

  • Alpha-hemolysin
  • Single molecule
  • Stochastic sensing
  • Structure
  • Unnatural amino acid

ASJC Scopus subject areas

  • General

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    Banerjee, A., Mikhailova, E., Cheley, S., Gu, L. Q., Montoya, M., Nagaoka, Y., Gouaux, E., & Bayley, H. (2010). Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores. Proceedings of the National Academy of Sciences of the United States of America, 107(18), 8165-8170. https://doi.org/10.1073/pnas.0914229107