Biological activities and structural properties of the atypical bacteriocins mesenterocin 52b and leucocin b-ta33a.
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.
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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, France.
Krier
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Mulliert
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Vitoux
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D000595:Amino Acid Sequence; D001430:Bacteriocins / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology*; D002942:Circular Dichroism; D007777:Lactobacillaceae / Q000187:drug effects* / Q000235:genetics / Q000254:growth & development; D007934:Leuconostoc / Q000187:drug effects / Q000254:growth & development / Q000378:metabolism; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D017433:Protein Structure, Secondary
D001430:Bacteriocins; D010455:Peptides; C432937:mesenterocin 52B; C071726:leucocin A-UAL 187