Molecular Imaging and Orientational Changes of Antimicrobial Peptides in Membranes
Resistance to conventional antibiotics has placed antimicrobial peptides under the spotlight as alternative therapeutics for microbial infections. However, the design of specific non-toxic peptides has been elusive due largely to our poor understanding of the precise mechanism of cell lysis. Specifically, the difficulty in defining peptide conformation and location in membranes needs to be addressed. We have used a combination of dual polarisation interferometry (DPI), surface plasmon resonance spectroscopy (SPR) and atomic force microscopy (AFM) to gain an unprecedented detailed molecular picture of membrane lysis by antimicrobial peptides.
Results and Discussion
Dual Polarisation Interferometry
DPI is a new optical biosensor that provides a measure of the thickness and density of the membrane upon peptide binding, which together with the kinetic data from SPR and the high resolution images from AFM, provides an integrated approach to delineating specific molecular...
KeywordsAtomic Force Microscopy Surface Plasmon Resonance Antimicrobial Peptide Interference Pattern Slab Waveguide
The support of the Australian Research Council is gratefully acknowledged.