Influence of environmental conditions on the interfacial organisation of fengycin, a bioactive lipopeptide produced by Bacillus subtilis

Physicochemical characterisation of four peptide sequences related to thrombospondin-1B

“…Maxima pressures achieved are closely similar to those described in [12] for a 24 Aa peptide, although extrapolated area/ molecule values are smaller in our case, suggesting a random coil structure. Moreover, the shape and slope of isotherms are also similar to those described in previous papers [13][14][15]. The value of extrapolated area gives an indication of the cross-sectional area of the peptide chain lying at the interface.…”

Lipopeptides as main ingredients for inhibition of fungal phytopathogens by Bacillus subtilis/amyloliquefaciens

“…Such specificity regarding the target membrane could explain our observations on the variability of fungitoxicity level for each LP in function of the antagonist species. Additional research is needed to fully understand the precise mechanisms of action and membrane determinants in cell sensitivity to fengycin and iturins (including mycosubtilins and bacillomycins) but it still clearly appeared that it depends on both the anionic nature of phospholipids, the presence of sphingomyelin and the type and content in sterols (Avis and Bélanger, 2001;Deleu et al, 2008;Eeman et al, 2009;Nasir and Besson, 2011).…”

Flexible loops of thread-like micelles are formed upon interaction of l-α-dimyristoyl-phosphatidylcholine with the biosurfactant surfactin as revealed by cryo-electron tomography

“…During the last decade great progress has also been achieved with regard to the visualization of lipid-biosurfactant aggregates using advanced TEM- [20,44,45] and AFM- [22][23][24][25]46] techniques. For example, similar results have been reported for the interaction of fengycins with phospholipid membranes [45].…”