Vol 4: Real-time Measurement of Membrane Conformational States Induced by Antimicrobial Peptides: Balance Between Recovery and Lysis.Report as inadecuate



 Vol 4: Real-time Measurement of Membrane Conformational States Induced by Antimicrobial Peptides: Balance Between Recovery and Lysis.


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This article is from Scientific Reports, volume 4.AbstractThe disruption of membranes by antimicrobial peptides is a multi-state process involving significant structural changes in the phospholipid bilayer. However, direct measurement of these membrane structural changes is lacking. We used a combination of dual polarisation interferometry DPI, surface plasmon resonance spectroscopy SPR and atomic force microscopy AFM to measure the real-time changes in membrane structure through the measurement of birefringence during the binding of magainin 2 Mag2 and a highly potent analogue in which Ser8, Gly13 and Gly18 has been replaced with alanine Mag-A. We show that the membrane bilayer undergoes a series of structural changes upon peptide binding before a critical threshold concentration is reached which triggers a significant membrane disturbance. We also propose a detailed model for antimicrobial peptide action as a function of the degree of bilayer disruption to provide an unprecedented in-depth understanding of the membrane lysis in terms of the interconversion of different membrane conformational states in which there is a balance between recovery and lysis.



Author: Hall, Kristopher; Lee, Tzong-Hsien; Mechler, Adam I.; Swann, Marcus J.; Aguilar, Marie-Isabel

Source: https://archive.org/







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