[Ala4]surfactin, a novel isoform from Bacillus subtilis studied by mass and NMR spectroscopies.

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.
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Journal articles
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https://hal.archives-ouvertes.fr/hal-02082597
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Submitted on : Thursday, March 28, 2019 - 12:32:59 PM
Last modification on : Friday, March 29, 2019 - 2:38:15 AM

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  • HAL Id : hal-02082597, version 1
  • PUBMED : 8076655

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M Peypoux, J.M Bonmatin, H Labbe, G Grangemard, B Das, et al.. [Ala4]surfactin, a novel isoform from Bacillus subtilis studied by mass and NMR spectroscopies.. European Journal of Biochemistry, Wiley, 1994, 224 (1), pp.89-96. ⟨hal-02082597⟩

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