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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2011-6-17
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pubmed:abstractText |
We compared the abilities of structurally related cationic cyclodextrins to inhibit Bacillus anthracis lethal toxin and Staphylococcus aureus ?-hemolysin. We found that both ?- and ?-cyclodextrin derivatives effectively inhibited anthrax toxin action by blocking the transmembrane oligomeric pores formed by the protective antigen (PA) subunit of the toxin, whereas ?-cyclodextrins were ineffective. In contrast, ?-hemolysin was selectively blocked only by ?-cyclodextrin derivatives, demonstrating that both symmetry and size of the inhibitor and the pore are important.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1098-6596
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
55
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3594-7
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pubmed:meshHeading |
pubmed-meshheading:21555769-Animals,
pubmed-meshheading:21555769-Antigens, Bacterial,
pubmed-meshheading:21555769-Bacterial Toxins,
pubmed-meshheading:21555769-Cell Death,
pubmed-meshheading:21555769-Cell Line,
pubmed-meshheading:21555769-Hemolysin Proteins,
pubmed-meshheading:21555769-Molecular Conformation,
pubmed-meshheading:21555769-Staphylococcus aureus,
pubmed-meshheading:21555769-alpha-Cyclodextrins,
pubmed-meshheading:21555769-beta-Cyclodextrins,
pubmed-meshheading:21555769-gamma-Cyclodextrins
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pubmed:year |
2011
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pubmed:articleTitle |
Symmetry requirements for effective blocking of pore-forming toxins: comparative study with alpha-, beta-, and gamma-cyclodextrin derivatives.
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pubmed:affiliation |
Institute of Physical Chemistry, National Center for Scientific Research Demokritos, Aghia Paraskevi 15310, Athens, Greece.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural,
Research Support, N.I.H., Intramural
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