Journal list menu

Volume 224, Issue 1 p. 89-96
Free Access

[Ala4]Surfactin, a Novel Isoform from Bacillus subtilis Studied by Mass and NMR Spectroscopies

Françoise Peypoux

Corresponding Author

Françoise Peypoux

Laboratoire de Biochimie Microbienne, Université Claude Bernard Lyon 1, France

Laboratoire de Biochimie Analytique et Synthèse Bioorganique, Université Claude Bernard Lyon I, France

Correspondence to F. Peypoux, Laboratoire de Biochimie Microbienne, Université Claude Bernard Lyon 1, 43 Boulevard du 11 Novembre 1918, F-69622 Villeurbanne Cedex, FranceSearch for more papers by this author
Jean-Marc Bonmatin

Jean-Marc Bonmatin

Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique and Université d'Orléans, Orléans, France

Search for more papers by this author
Henri Labbe

Henri Labbe

Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique and Université d'Orléans, Orléans, France

Search for more papers by this author
Isabelle Grangemard

Isabelle Grangemard

Laboratoire de Biochimie Analytique et Synthèse Bioorganique, Université Claude Bernard Lyon I, France

Search for more papers by this author
Bhupesh C. Das

Bhupesh C. Das

Institut de Chimie des Substances Naturelles, Gif-sur-Yvette, France

Search for more papers by this author
Marius Ptak

Marius Ptak

Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique and Université d'Orléans, Orléans, France

Search for more papers by this author
Jean Wallach

Jean Wallach

Laboratoire de Biochimie Analytique et Synthèse Bioorganique, Université Claude Bernard Lyon I, France

Search for more papers by this author
Georges Michel

Georges Michel

Laboratoire de Biochimie Microbienne, Université Claude Bernard Lyon 1, France

Search for more papers by this author
First published: August 1994
Citations: 70

Abstract

When Bacillus subtilis S 499 was grown on a culture medium containing L-alanine as nitrogen source, a mixture of surfactins was obtained. Suitable chromatographic conditions allowed the separation of isoforms. Among these compounds, a new variant of surfactin was isolated and its structure was established by chemical and spectrometric methods, especially by NMR spectrometry. It contains a peptide sequence which differs from that of standard surfactin by the replacement of the L-valine residue by L-alanine residue in position 4. The folding mode of [Ala4]surfactin as deduced from NMR results was compared with that of standard surfactin and the structure/properties relationship issuing from the study of this new isoform is discussed.

Abbreviations

  • [Ala4]Surfactin
  • surfactin in which Val4 has been replaced by Ala
  • LSIMS
  • liquid secondary ion mass spectrometry
  • DQF-COSY
  • double-quantum-filter correlation spectroscopy
  • TOCSY
  • total correlation spectroscopy
  • NOESY
  • nuclear Overhauser enhancement spectroscopy
  • γCMC
  • surface tension close to the critical micellar concentration