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Iturin lipopeptide is a cyclic heptapeptide molecules, exhibits strong in vitro antifungal activity through the formation of ion-conducting pores on fungal membranes. In particular, its activity against phytopathogenic fungi has sparked interest in its application as a biofungicide in agriculture. These lipopeptide molecules are of appreciable interest because of their biological as well as physico-chemical properties, which can be exploited in food, oil and pharmaceutical industries. All strains of Bacillus subtilis produce lipopeptides of the Iturin family.
STRUCTURE
STRUCTURE
Iturin lipopeptide is a cyclic peptide of 7 amino acids linked to a fatty acid chain that can vary from C-14 to C-17 carbon molecules. Iturin A, iturin AL, subtulene A, and mycosubtilin all share the same peptide backbone while carrying different hydrophobic side chains.
Studies reported four iturin antibiotics (iturin A, C, D, E), five bacillomycins and mycosubtilin are known. There are reports showing antifungal activity of the bacillomycins is strongly dependent on the chain length and supporting the mode of action against fungal pathogens.
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