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pubmed-article:15493921pubmed:abstractTextA key factor in the potential clinical utility of membrane-active antibiotics is their cell selectivity (i.e., prokaryote over eukaryote). Cationic steroid antibiotics were developed to mimic the lipid A binding character of polymyxin B and are shown to bind lipid A derivatives with affinity greater than that of polymyxin B. The outer membranes of Gram-negative bacteria are comprised primarily of lipid A, and a fluorophore-appended cationic steroid antibiotic displays very high selectivity for Gram-negative bacterial membranes over Gram-positive bacteria and eukaryotic cell membranes. This cell selectivity of cationic steroid antibiotics may be due, in part, to the affinity of these compounds for lipid A.lld:pubmed
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pubmed-article:15493921pubmed:copyrightInfoCopyright 2004 American Chemical Societylld:pubmed
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pubmed-article:15493921pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15493921pubmed:articleTitleOrigins of cell selectivity of cationic steroid antibiotics.lld:pubmed
pubmed-article:15493921pubmed:affiliationContribution from the Department of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, USA.lld:pubmed
pubmed-article:15493921pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15493921pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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