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Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers

by Judge, Peter J. , Jiang, Haibo , Koksch, Beate , Hoogenboom, Bart W. , Ray, Santanu , Pyne, Alice , Lamarre, Baptiste , Ravi, Jascindra , Watts, Anthony , Martyna, Glenn J. , Gerling, Ulla I. M. , Carr, Matthew , Crain, Jason , Ryadnov, Maxim G. , Grovenor, Chris R. M. , Rakowska, Paulina D.

in Amino Acid Sequence / Antimicrobial agents / Antimicrobial Cationic Peptides - chemistry / Antimicrobial Cationic Peptides - genetics / Antimicrobial Cationic Peptides - metabolism / antimicrobial peptides / Antimicrobials / Atomic force microscopy / Biochemistry / Biological Sciences / Chromatography, High Pressure Liquid / Circular Dichroism / image analysis / Imaging / Line spectra / Lipid bilayers / Lipid Bilayers - chemistry / Lipids / Magnetic Resonance Spectroscopy / Mass Spectrometry / Membranes / Microscopy / Microscopy, Atomic Force / Molecular Dynamics Simulation / Molecular Sequence Data / Nanotechnology - methods / P branes / Peptides / Phospholipids / Phospholipids - chemistry / Phospholipids - metabolism / Physical Sciences / Pores / Protein Engineering / Proteins / Research facilities / Scientific imaging / Spectrometry, Mass, Secondary Ion

2013

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Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers

2013

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2013

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Journal Article

Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers

Judge, Peter J.,

Jiang, Haibo,

Koksch, Beate,

Hoogenboom, Bart W.,

Ray, Santanu,

Pyne, Alice,

Lamarre, Baptiste,

Ravi, Jascindra,

Watts, Anthony,

Martyna, Glenn J.,

Gerling, Ulla I. M.,

Carr, Matthew,

Crain, Jason,

Ryadnov, Maxim G.,

Grovenor, Chris R. M.,

Rakowska, Paulina D.

2013

Overview

Antimicrobial peptides are postulated to disrupt microbial phospholipid membranes. The prevailing molecular model is based on the formation of stable or transient pores although the direct observation of the fundamental processes is lacking. By combining rational peptide design with topographical (atomic force microscopy) and chemical (nanoscale secondary ion mass spectrometry) imaging on the same samples, we show that pores formed by antimicrobial peptides in supported lipid bilayers are not necessarily limited to a particular diameter, nor they are transient, but can expand laterally at the nano-to-micrometer scale to the point of complete membrane disintegration. The results offer a mechanistic basis for membrane poration as a generic physicochemical process of cooperative and continuous peptide recruitment in the available phospholipid matrix.

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Publisher

National Academy of Sciences,National Acad Sciences

Subject

Amino Acid Sequence

/ Antimicrobial agents

/ Antimicrobial Cationic Peptides - chemistry

/ Antimicrobial Cationic Peptides - genetics

/ Antimicrobial Cationic Peptides - metabolism

/ antimicrobial peptides

/ Antimicrobials