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Biological activities and structural properties of the atypical bacteriocins mesenterocin 52b and leucocin b-ta33a.


ABSTRACT: 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.

SUBMITTER: Corbier C 

PROVIDER: S-EPMC92749 | biostudies-other | 2001 Apr

REPOSITORIES: biostudies-other

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Biological activities and structural properties of the atypical bacteriocins mesenterocin 52b and leucocin b-ta33a.

Corbier C C   Krier F F   Mulliert G G   Vitoux B B   Revol-Junelles A M AM  

Applied and environmental microbiology 20010401 4


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. ...[more]

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