| pubmed-article:16861271 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16861271 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:16861271 | lifeskim:mentions | umls-concept:C0023768 | lld:lifeskim |
| pubmed-article:16861271 | lifeskim:mentions | umls-concept:C0332528 | lld:lifeskim |
| pubmed-article:16861271 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:16861271 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:16861271 | lifeskim:mentions | umls-concept:C0300260 | lld:lifeskim |
| pubmed-article:16861271 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:16861271 | pubmed:dateCreated | 2006-9-25 | lld:pubmed |
| pubmed-article:16861271 | 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. | lld:pubmed |
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| pubmed-article:16861271 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16861271 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16861271 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16861271 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16861271 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16861271 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16861271 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:16861271 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:16861271 | pubmed:author | pubmed-author:MaBuyongB | lld:pubmed |
| pubmed-article:16861271 | pubmed:author | pubmed-author:NussinovRuthR | lld:pubmed |
| pubmed-article:16861271 | pubmed:author | pubmed-author:JangHyunbumH | lld:pubmed |
| pubmed-article:16861271 | pubmed:author | pubmed-author:WoolfThomas... | lld:pubmed |
| pubmed-article:16861271 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16861271 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:16861271 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:16861271 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16861271 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16861271 | pubmed:pagination | 2848-59 | lld:pubmed |
| pubmed-article:16861271 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:16861271 | pubmed:meshHeading | pubmed-meshheading:16861271... | lld:pubmed |
| pubmed-article:16861271 | pubmed:meshHeading | pubmed-meshheading:16861271... | lld:pubmed |
| pubmed-article:16861271 | pubmed:meshHeading | pubmed-meshheading:16861271... | lld:pubmed |
| pubmed-article:16861271 | pubmed:meshHeading | pubmed-meshheading:16861271... | lld:pubmed |
| pubmed-article:16861271 | pubmed:meshHeading | pubmed-meshheading:16861271... | lld:pubmed |
| pubmed-article:16861271 | pubmed:meshHeading | pubmed-meshheading:16861271... | lld:pubmed |
| pubmed-article:16861271 | pubmed:meshHeading | pubmed-meshheading:16861271... | lld:pubmed |
| pubmed-article:16861271 | pubmed:meshHeading | pubmed-meshheading:16861271... | lld:pubmed |
| pubmed-article:16861271 | pubmed:meshHeading | pubmed-meshheading:16861271... | lld:pubmed |
| pubmed-article:16861271 | pubmed:meshHeading | pubmed-meshheading:16861271... | lld:pubmed |
| pubmed-article:16861271 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16861271 | pubmed:articleTitle | Interaction of protegrin-1 with lipid bilayers: membrane thinning effect. | lld:pubmed |
| pubmed-article:16861271 | pubmed:affiliation | Center for Cancer Research Nanobiology Program, SAIC-Frederick, Inc., NCI-Frederick, Frederick, Maryland 21702, USA. | lld:pubmed |
| pubmed-article:16861271 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16861271 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:16861271 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| pubmed-article:16861271 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
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