- 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 ...
Expand abstract - Publication status:
- Published
- 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
- Language:
- English
- Keywords:
- Copyright date:
- 2000
Journal article
Reversal of charge selectivity in transmembrane protein pores by using noncovalent molecular adapters.
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