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Abstract / Description of output
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 language | English |
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Pages (from-to) | 8918-8923 |
Number of pages | 6 |
Journal | Proceedings of the National Academy of Sciences (PNAS) |
Volume | 110 |
Issue number | 22 |
Early online date | 13 May 2013 |
DOIs | |
Publication status | Published - 28 May 2013 |
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Dive into the research topics of 'Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers'. Together they form a unique fingerprint.Projects
- 1 Finished
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Structure-Function Studies of Antimicrobial and Fusogenic peptides by solid state NMR Spectroscopy and MD Simulation
Crain, J.
1/06/11 → 31/05/14
Project: Research