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Applied and Environmental Microbiology, April 2001, p. 1418-1422, Vol. 67, No. 4
Laboratoire de Cristallographie et
Modélisation des Matériaux Minéraux et Biologiques,
Groupe Biocristallographie, UPRESA CNRS 7036, Université Henri
Poincaré-Nancy I, 54506 Vandoeuvre-lès-Nancy
cedex,1 and Laboratoire de
Bioprocédés Agro-Alimentaires, Ecole Nationale
Supérieure d'Agronomie et des Industries Alimentaires
Received 27 July 2000/Accepted 17 January 2001
The antibacterial spectra and modes of action of
synthetic peptides corresponding to mesenterocin 52B and leucocin
B-TA33a greatly differ despite their high sequence homology. Circular dichroism experiments establish the capacity of each of these two
peptides to partly fold into an amphiphilic helix that might be crucial
for their adsorption at lipophilic-hydrophilic interfaces.
0099-2240/01/$04.00+0 DOI: 10.1128/AEM.67.4.1418-1422.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Biological Activities and Structural Properties of
the Atypical Bacteriocins Mesenterocin 52B and Leucocin
B-TA33a
Institut
National Polytechnique de Lorraine (ENSAIA-INPL), 54505 Vandoeuvre-lès-Nancy cedex,2 France
*
Corresponding author. Mailing address: Laboratoire de
Bioprocédés Agro-Alimentaires, Ecole Nationale
Supérieure d'Agronomie et des Industries Alimentaires
Institut
National Polytechnique de Lorraine (ENSAIA-INPL), 2, Avenue de la
Forêt de Haye, 54505 Vandoeuvre-lès-Nancy cedex, France.
Phone: 00 33 3 83 59 58 84. Fax: 00 33 3 83 59 58 04. E-mail:
Anne-Marie.Revol{at}ensaia.inpl-nancy.fr.
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