Scientific Correspondence

Nature 398, 383-384 (1 April 1999) | doi:10.1038/18803

Molecular basis of triclosan activity

Colin W. Levy1, Anna Roujeinikova1, Svetlana Sedelnikova1, Patrick J. Baker1, Antoine R. Stuitje2, Antoni R. Slabas3, David W. Rice1 & John B. Rafferty1

Triclosan (5-chloro-2-(2,4-dichlorophenoxy) phenol) has been used for more than 30 years as a general antibacterial and antifungal agent, and is found in formulations as diverse as toothpastes, cosmetics, antiseptic soaps, carpets, plastic kitchenware and toys. It has recently been suggested that triclosan blocks lipid biosynthesis by specifically inhibiting the enzyme enoyl-acyl carrier protein reductase (ENR)1. We have carried out a structural analysis and inhibition experiments on a complex of ENR from the bacterium Escherichia coli with triclosan and NAD+. We find that triclosan acts as a site-directed, very potent inhibitor of the enzyme by mimicking its natural substrate.

  1. Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK
  2. Department of Genetics, Institute of Molecular Biological Studies (IMBW), Vrije Universiteit, Biocenter Amsterdam, 1081 HV Amsterdam, The Netherlands
  3. Department of Biological Sciences, University of Durham, Durham DH1 3LE, UK
    e-mail: Email: d.rice@sheffield.ac.uk