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• W2008451855 abstract "Cyclodextrins act as noncovalent molecular adapters when lodged in the lumen of the α-hemolysin (αHL) pore. The adapters act as binding sites for channel blockers, thereby offering a basis for the detection of a variety of organic molecules with αHL as a biosensor element. To further such studies, it is important to find conditions under which the dwell time of cyclodextrins in the lumen of the pore is extended. Here, we use single-channel recording to explore the pH- and voltage-dependence of the interaction of β-cyclodextrin (βCD) with αHL. βCD can access its binding site only from the trans entrance of pores inserted from the cis side of a bilayer. Analysis of the binding kinetics shows that there is a single binding site for βCD, with an apparent equilibrium dissociation constant that varies by >100-fold under the conditions explored. The dissociation rate constant for the neutral βCD molecule varies with pH and voltage, a result that is incompatible with two states of the αHL pore, one of high and the other of low affinity. Rather, the data suggest that the actual equilibrium dissociation constant for the αHL ·βCD complex varies continuously with the transmembrane potential." @default.
• W2008451855 created "2016-06-24" @default.
• W2008451855 creator A5065179718 @default.
• W2008451855 creator A5080903560 @default.
• W2008451855 date "2000-10-01" @default.
• W2008451855 modified "2023-10-18" @default.
• W2008451855 title "Interaction of the Noncovalent Molecular Adapter, β-Cyclodextrin, with the Staphylococcal α-Hemolysin Pore" @default.
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• W2008451855 doi "https://doi.org/10.1016/s0006-3495(00)76445-9" @default.
• W2008451855 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1301087" @default.
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