Modulation of lipid membrane structural and mechanical properties by a peptidomimetic derived from reduced amide scaffold.

摘要: Understanding how antimicrobial peptidomimetics interact with lipid membranes is important in battling multidrug resistant bacterial pathogens. We study the effects of a recently reported peptidomimetic on bilayer structural and mechanical properties. The compound referred to as E107-3 synthesized based acylated reduced amide scaffold has been shown exhibit good potency. Our vesicle leakage assay indicates that increases permeability. use micropipette aspiration explore kinetic response giant unilamellar vesicles (GUVs). Exposure causes GUV protrusion length LP spontaneously increase then decrease, followed by rupture. Solution atomic force microscopy (AFM) used visualize modulation within nanoscopic regime. Unlike melittin, which produces pore-like structures, found induce heterogeneous structures. Finally, we AFM-based spectroscopy impact find incremental addition planar bilayers results moderate decrease puncture FP 39% area compressibility modulus KA. To explain our experimental data, propose membrane interaction model encompassing disruption chain packing extraction molecules. later action mode supported observation double-bilayer structure presence fusogenic calcium ions.