Abstract:
: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.
journal_name
Proc Natl Acad Sci U S Aauthors
Rakowska PD,Jiang H,Ray S,Pyne A,Lamarre B,Carr M,Judge PJ,Ravi J,Gerling UI,Koksch B,Martyna GJ,Hoogenboom BW,Watts A,Crain J,Grovenor CR,Ryadnov MGdoi
10.1073/pnas.1222824110subject
Has Abstractpub_date
2013-05-28 00:00:00pages
8918-23issue
22eissn
0027-8424issn
1091-6490pii
1222824110journal_volume
110pub_type
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