Electroosmotic enhancement of the binding of a neutral molecule to a transmembrane pore.

Journal article

The flux of solvent water coupled to the transit of ions through protein pores is considerable. The effect of this electroosmotic solvent flow on the binding of a neutral molecule [beta-cyclodextrin (betaCD)] to sites within the staphylococcal alpha-hemolysin pore was investigated. Mutant alpha-hemolysin pores were used to which betaCD can bind from either entrance and through which the direction of water flow can be controlled by choosing the charge selectivity of the pore and the polarity o...

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Authors: Gu, L; Cheley, S; Bayley, H

• Publication status: Published
• Journal: Proceedings of the National Academy of Sciences of the United States of America
• Volume: 100
• Issue: 26
• Pages: 15498-15503
• Publication date: 2003-12-01
• DOI: 10.1073/pnas.2531778100
• EISSN: 1091-6490
• ISSN: 0027-8424
• Language: English
• Keywords: beta-Cyclodextrins; Binding Sites; Osmosis; Models, Molecular; Recombinant Proteins; Staphylococcus; Hemolysin Proteins; Bacterial Toxins; Cyclodextrins; Protein Subunits; Electrochemistry; Mutagenesis, Site-Directed