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    Catalyzing the Translocation of Polypeptides through Attractive Interactions
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    Contribution from the Department of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, United Kingdom, and Structural Biology, Biochemistry, and Biophysics Program, Syracuse University, 111 College Place, Syracuse, New York 13244-4100
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2007, 129, 45, 14034–14041
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    https://doi.org/10.1021/ja0749340
    Published October 19, 2007
    Copyright © 2007 American Chemical Society
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    Abstract

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    Facilitated translocation of polypeptides through a protein pore is a ubiquitous and fundamental process in biology. Several translocation systems possess various well-defined binding sites within the pore lumen, but a clear mechanistic understanding of how the interaction of the polypeptides with the binding site alters the underlying kinetics is still missing. Here, we employed rational protein design and single-channel electrical recordings to obtain detailed kinetic signatures of polypeptide translocation through the staphylococcal α-hemolysin (αHL) transmembrane pore, a robust, tractable, and versatile β-barrel protein. Acidic binding sites composed of rings of negatively charged aspartic acid residues, engineered at strategic positions within the β barrel, produced dramatic changes in the functional properties of the αHL protein, facilitating the transport of cationic polypeptides from one side of the membrane to the other. When two electrostatic binding sites were introduced, at the entry and exit of the β barrel, both the rate constants of association and dissociation increased substantially, diminishing the free energy barrier for translocation. By contrast, more hydrophobic polypeptides exhibited a considerable decrease in the rate constant of association to the pore lumen, having to overcome a greater energetic barrier because of the hydrophilic nature of the pore interior.

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    †

     Department of Physics, Syracuse University.

    ‡

     University of Oxford.

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    In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

    §

     Structural Biology, Biochemistry, and Biophysics Program, Syracuse University.

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    Detailed I/V profiles for the wild-type and engineered αHL protein pores, ionic selectivity of the wild-type and engineered αHL protein pores, parameters of the transient current blockades, circular dichroism measurements of the polypeptides. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Cite this: J. Am. Chem. Soc. 2007, 129, 45, 14034–14041
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