Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers

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

    Research output: Contribution to journalArticlepeer-review


    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 completemembrane disintegration. The results offer a mechanistic basis for membrane poration as a generic physicochemical process of cooperative and continuous peptide recruitment in the available phospholipidmatrix.

    Original languageEnglish
    Pages (from-to)8918-8923
    Number of pages6
    JournalProceedings of the National Academy of Sciences of the United States of America
    Issue number22
    Publication statusPublished - 28 May 2013


    • Antibiotics
    • De novo protein design
    • Innate host defense
    • Nanometrology
    • Nanoscopy


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