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Journal article

Membrane pore formation at protein-lipid interfaces.

Abstract:

Pore-forming proteins (PFPs) interact with lipid bilayers to compromise membrane integrity. Many PFPs function by inserting a ring of oligomerized subunits into the bilayer to form a protein-lined hydrophilic channel. However, mounting evidence suggests that PFPs can also generate 'proteolipidic' pores by contributing to the fusion of inner and outer bilayer leaflets to form a toroidal structure. We discuss here toroidal pore formation by peptides including melittin, protegrin, and Alzheimer'...

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Publication status:
Published

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Publisher copy:
10.1016/j.tibs.2014.09.002

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
Journal:
Trends in biochemical sciences More from this journal
Volume:
39
Issue:
11
Pages:
510-516
Publication date:
2014-11-01
DOI:
EISSN:
1362-4326
ISSN:
0968-0004
Language:
English
Keywords:
Pubs id:
pubs:492028
UUID:
uuid:f60f9ca8-13e8-42ff-bc58-26408ee90c7b
Local pid:
pubs:492028
Source identifiers:
492028
Deposit date:
2014-12-15

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