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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2006-9-25
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pubmed:abstractText |
Protegrins (PG) are important in defending host tissues, preventing infection via an attack on the membrane surface of invading microorganisms. Protegrins have powerful antibiotic abilities, but the molecular-level mechanisms underlying the interactions of their beta-sheet motifs with the membrane are not known. Protegrin-1 (PG-1) is composed of 18 amino acids with a high content of basic residues and two disulfide bonds. Here we focused on the stability of PG-1 at the amphipathic interface in lipid bilayers and on the details of the peptide-membrane interactions. We simulated all-atom models of the PG-1 monomer with explicit water and lipid bilayers composed of both homogeneous POPC (palmitoyl-oleyl-phosphatidylcholine) lipids and a mixture of POPC/POPG (palmitoyl-oleyl-phosphatidylglycerol) (4:1) lipids. We observed that local thinning of the lipid bilayers mediated by the peptide is enhanced in the lipid bilayer containing POPG, consistent with experimental results of selective membrane targeting. The beta-hairpin motif of PG-1 is conserved in both lipid settings, whereas it is highly bent in aqueous solution. The conformational dynamics of PG-1, especially the highly charged beta-hairpin turn region, are found to be mostly responsible for disturbing the membrane. Even though the eventual membrane disruption requires PG-1 oligomers, our simulations clearly show the first step of the monomeric effects. The thinning effects in the bilayer should relate to pore/channel formation in the lipid bilayer and thus be responsible for further defects in the membrane caused by oligomer.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-10223293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-10446287,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-10585936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-10590301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-10837335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-11102868,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-11566791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-11853682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-12022262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-12146951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-12238928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-12379126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-12423203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-12738879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-12770881,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-14507700,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-14515159,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-14556740,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-14653713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-15240452,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-15465855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-15519318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-15542560,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-15596510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-15695635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-15738465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-15783230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-16040748,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-16183881,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-16201813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-16222654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-16235232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-16297931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-7526400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-7547876,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-8075068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-8807886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-9370432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-9449316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-9468319,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-9573496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-9635744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16861271-9746504
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2848-59
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16861271-Antimicrobial Cationic Peptides,
pubmed-meshheading:16861271-Computer Simulation,
pubmed-meshheading:16861271-Lipid Bilayers,
pubmed-meshheading:16861271-Models, Molecular,
pubmed-meshheading:16861271-Peptides,
pubmed-meshheading:16861271-Phosphatidylcholines,
pubmed-meshheading:16861271-Phosphatidylglycerols,
pubmed-meshheading:16861271-Protein Structure, Secondary,
pubmed-meshheading:16861271-Proteins,
pubmed-meshheading:16861271-Water
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pubmed:year |
2006
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pubmed:articleTitle |
Interaction of protegrin-1 with lipid bilayers: membrane thinning effect.
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pubmed:affiliation |
Center for Cancer Research Nanobiology Program, SAIC-Frederick, Inc., NCI-Frederick, Frederick, Maryland 21702, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural,
Research Support, N.I.H., Intramural
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