Abstract
N-Chlorotaurine sodium (NCT) is a promising microbicidal agent for topical treatment of infections. Its targets of attack in Escherichia coli have been investigated by proteomics. Incubation in 1% NCT for 10 and 30 min revealed a change of the charge and a separation of numerous proteins into a series of spots with a different pI. Charge differences could be related to oxidation of cysteine residues to their corresponding sulfonic acids. Heat shock protein 60 appeared, while ribosome-releasing factor, d-ribose periplasmic binding protein, and malonyl-CoA transacylase spots decreased. These results indicate penetration of oxidation capacity into the bacteria and destruction of essential proteins by NCT.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Acyl-Carrier Protein S-Malonyltransferase / metabolism
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Bacterial Proteins / drug effects
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Chaperonin 60 / metabolism
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Cysteine / chemistry
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Electrophoresis, Gel, Two-Dimensional
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Enzyme Inhibitors / pharmacology*
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Escherichia coli / drug effects*
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Escherichia coli / metabolism*
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Oxidation-Reduction
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Periplasmic Binding Proteins / metabolism
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Protein Serine-Threonine Kinases / antagonists & inhibitors*
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Proteomics*
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Ribosomal Proteins / metabolism
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Spectrometry, Mass, Electrospray Ionization
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Sulfonic Acids / metabolism
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Taurine / analogs & derivatives*
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Taurine / pharmacology
Substances
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Bacterial Proteins
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Chaperonin 60
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Enzyme Inhibitors
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Periplasmic Binding Proteins
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Ribosomal Proteins
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Sulfonic Acids
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ribosome releasing factor
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Taurine
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N-chlorotaurine
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Acyl-Carrier Protein S-Malonyltransferase
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Protein Serine-Threonine Kinases
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Cysteine