| Autor: |
Rakowska PD; National Physical Laboratory, Teddington TW11 0LW, United Kingdom., 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 MG |
| Jazyk: |
angličtina |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2013 May 28; Vol. 110 (22), pp. 8918-23. Date of Electronic Publication: 2013 May 13. |
| DOI: |
10.1073/pnas.1222824110 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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