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Reversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters.

Abstract:

In this study, the charge selectivity of staphylococcal alpha-hemolysin (alphaHL), a bacterial pore-forming toxin, is manipulated by using cyclodextrins as noncovalent molecular adapters. Anion-selective versions of alphaHL, including the wild-type pore and various mutants, become more anion selective when beta-cyclodextrin (betaCD) is lodged within the channel lumen. By contrast, the negatively charged adapter, hepta-6-sulfato-beta-cyclodextrin (s(7)betaCD), produces cation selectivity. The ...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.97.8.3959

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Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
97
Issue:
8
Pages:
3959-3964
Publication date:
2000-04-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:798f09e3-24e5-4c4a-a038-add9c3e10d7d
Source identifiers:
52188
Local pid:
pubs:52188

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