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Start Over Author "Sarg, Bettina" Journal proteomics
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4. Protein sites of attack of N-chlorotaurine in Escherichia coli.

Author

Arnitz R, Sarg B, Ott HW, Neher A, Lindner H, and Nagl M

Subjects
Acyl-Carrier Protein S-Malonyltransferase metabolism, Bacterial Proteins drug effects, Chaperonin 60 metabolism, Cysteine chemistry, Electrophoresis, Gel, Two-Dimensional, Oxidation-Reduction, Periplasmic Binding Proteins metabolism, Ribosomal Proteins metabolism, Spectrometry, Mass, Electrospray Ionization, Sulfonic Acids metabolism, Taurine pharmacology, Enzyme Inhibitors pharmacology, Escherichia coli drug effects, Escherichia coli metabolism, Protein Serine-Threonine Kinases antagonists & inhibitors, Proteomics, Taurine analogs & derivatives
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.

Published
2006
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