Biological Activities and Structural Properties of the Atypical Bacteriocins Mesenterocin 52B and Leucocin B-TA33a
AUTOR(ES)
Corbier, C.
FONTE
American Society for Microbiology
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=92749Documentos Relacionados
- Variations in the Membrane Fatty Acid Composition of Resistant or Susceptible Leuconostoc or Weissella Strains in the Presence or Absence of Mesenterocin 52A and Mesenterocin 52B Produced by Leuconostoc mesenteroides subsp. mesenteroides FR52
- Some Structural and Biological Properties of Brucella Endotoxin
- Biological activities of toxins A and B of Clostridium difficile.
- Study of Structural and Electric Properties of the PZT 52/48 Doped With Er+3
- Biological glass fibers: Correlation between optical and structural properties