Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers

Jason Crain, Max Ryadnov, Chris Grosvener, Anthony Watts, Paulina Rakowska, Haibo Jiang, Matthew Carr, Glenn Martyna, Peter Judge

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 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.
Original languageEnglish
Pages (from-to)8918-8923
Number of pages6
JournalProceedings of the National Academy of Sciences
Issue number22
Early online date13 May 2013
Publication statusPublished - 28 May 2013


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