Abstract:
: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 of the applied potential. The Kd values for betaCD for individual mutant pores varied by >100-fold with the applied potential over a range of -120 to +120 mV. In all cases, the signs of the changes in binding free energy and the influence of potential on the association and dissociation rate constants for betaCD were consistent with an electroosmotic effect.
journal_name
Proc Natl Acad Sci U S Aauthors
Gu LQ,Cheley S,Bayley Hdoi
10.1073/pnas.2531778100keywords:
subject
Has Abstractpub_date
2003-12-23 00:00:00pages
15498-503issue
26eissn
0027-8424issn
1091-6490pii
2531778100journal_volume
100pub_type
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