Abstract:
:The antibacterial activity of many small, positively charged peptides and proteins is based on pore formation in lipid bilayers. It is here proposed to arise from an electroporation effect. This hypothesis is supported by calculations of the electrostatic potential of NK-lysin associated to a membrane. For a significant area of the protein-membrane interface, the electrostatic potential is found to be above the minimum threshold for electroporation. A single highly charged alpha-helical segment of NK-lysin is mainly responsible for this effect. It is experimentally demonstrated that a peptide comprising this helix has antibacterial activity. We propose that superficial association to membranes suffices to trigger electroporation, provided the peptide is sufficiently charged. The effect is referred to as molecular electroporation.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Miteva M,Andersson M,Karshikoff A,Otting Gdoi
10.1016/s0014-5793(99)01520-3keywords:
subject
Has Abstractpub_date
1999-11-26 00:00:00pages
155-8issue
1-2eissn
0014-5793issn
1873-3468pii
S0014-5793(99)01520-3journal_volume
462pub_type
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