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Biological activities and structural properties of the atypical bacteriocins mesenterocin 52B and leucocin B-TA33a
- Corbier, C., Krier, F., Mulliert, G., Vitoux, B., Revol-Junelles, A.M.
- Applied and environmental microbiology 2001 v.67 no.4 pp. 1418-1422
- bacteriocins, amino acid sequences, synthetic peptides, molecular conformation, antibacterial properties, Leuconostoc, lactic acid bacteria, spectroscopy, Weissella, protein secondary structure
- 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.