Structural effects of the antimicrobial peptide maculatin 1.1 on supported lipid bilayers
The interactions of the antimicrobial peptide maculatin 1.1 (GLFGVLAKVAAHVVPAIAEHF-NH 2 ) with model phospholipid membranes were studied by use of dual polarisation interferometry and neutron reflectometry and dimyristoylphosphatidylcholine (DMPC) and mixed DMPC–dimyristoylphosphatidylglycerol (DMPG...
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| Veröffentlicht in: | European biophysics journal 2013-01, Vol.42 (1), p.47-59 |
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| creator | Fernandez, David I. Le Brun, Anton P. Lee, Tzong-Hsien Bansal, Paramjit Aguilar, Marie-Isabel James, Michael Separovic, Frances |
| description | The interactions of the antimicrobial peptide maculatin 1.1 (GLFGVLAKVAAHVVPAIAEHF-NH
2
) with model phospholipid membranes were studied by use of dual polarisation interferometry and neutron reflectometry and dimyristoylphosphatidylcholine (DMPC) and mixed DMPC–dimyristoylphosphatidylglycerol (DMPG)-supported lipid bilayers chosen to mimic eukaryotic and prokaryotic membranes, respectively. In DMPC bilayers concentration-dependent binding and increasing perturbation of bilayer order by maculatin were observed. By contrast, in mixed DMPC–DMPG bilayers, maculatin interacted more strongly and in a concentration-dependent manner with retention of bilayer lipid order and structure, consistent with pore formation. These results emphasise the importance of membrane charge in mediating antimicrobial peptide activity and emphasise the importance of using complementary methods of analysis in probing the mode of action of antimicrobial peptides. |
| doi_str_mv | 10.1007/s00249-012-0796-6 |
| format | Article |
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) with model phospholipid membranes were studied by use of dual polarisation interferometry and neutron reflectometry and dimyristoylphosphatidylcholine (DMPC) and mixed DMPC–dimyristoylphosphatidylglycerol (DMPG)-supported lipid bilayers chosen to mimic eukaryotic and prokaryotic membranes, respectively. In DMPC bilayers concentration-dependent binding and increasing perturbation of bilayer order by maculatin were observed. By contrast, in mixed DMPC–DMPG bilayers, maculatin interacted more strongly and in a concentration-dependent manner with retention of bilayer lipid order and structure, consistent with pore formation. These results emphasise the importance of membrane charge in mediating antimicrobial peptide activity and emphasise the importance of using complementary methods of analysis in probing the mode of action of antimicrobial peptides.</description><identifier>ISSN: 0175-7571</identifier><identifier>EISSN: 1432-1017</identifier><identifier>DOI: 10.1007/s00249-012-0796-6</identifier><identifier>PMID: 22354331</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>Amphibian Proteins - chemistry ; Antimicrobial Cationic Peptides - chemistry ; Biochemistry ; Biological and Medical Physics ; Biomedical and Life Sciences ; Biophysics ; Cell Biology ; Dimyristoylphosphatidylcholine - chemistry ; Interferometry ; Life Sciences ; Lipid Bilayers - chemistry ; Membrane Biology ; Mode of action ; Nanotechnology ; Neurobiology ; Original Paper ; Peptides ; Phosphatidylglycerols - chemistry ; Static Electricity</subject><ispartof>European biophysics journal, 2013-01, Vol.42 (1), p.47-59</ispartof><rights>European Biophysical Societies' Association 2012</rights><rights>European Biophysical Societies' Association 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-ba3210a5334d4695a4301fecc3efa1b538f536dec58856ad3d00ef55b18b0a1f3</citedby><cites>FETCH-LOGICAL-c405t-ba3210a5334d4695a4301fecc3efa1b538f536dec58856ad3d00ef55b18b0a1f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00249-012-0796-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00249-012-0796-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22354331$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fernandez, David I.</creatorcontrib><creatorcontrib>Le Brun, Anton P.</creatorcontrib><creatorcontrib>Lee, Tzong-Hsien</creatorcontrib><creatorcontrib>Bansal, Paramjit</creatorcontrib><creatorcontrib>Aguilar, Marie-Isabel</creatorcontrib><creatorcontrib>James, Michael</creatorcontrib><creatorcontrib>Separovic, Frances</creatorcontrib><title>Structural effects of the antimicrobial peptide maculatin 1.1 on supported lipid bilayers</title><title>European biophysics journal</title><addtitle>Eur Biophys J</addtitle><addtitle>Eur Biophys J</addtitle><description>The interactions of the antimicrobial peptide maculatin 1.1 (GLFGVLAKVAAHVVPAIAEHF-NH
2
) with model phospholipid membranes were studied by use of dual polarisation interferometry and neutron reflectometry and dimyristoylphosphatidylcholine (DMPC) and mixed DMPC–dimyristoylphosphatidylglycerol (DMPG)-supported lipid bilayers chosen to mimic eukaryotic and prokaryotic membranes, respectively. In DMPC bilayers concentration-dependent binding and increasing perturbation of bilayer order by maculatin were observed. By contrast, in mixed DMPC–DMPG bilayers, maculatin interacted more strongly and in a concentration-dependent manner with retention of bilayer lipid order and structure, consistent with pore formation. These results emphasise the importance of membrane charge in mediating antimicrobial peptide activity and emphasise the importance of using complementary methods of analysis in probing the mode of action of antimicrobial peptides.</description><subject>Amphibian Proteins - chemistry</subject><subject>Antimicrobial Cationic Peptides - chemistry</subject><subject>Biochemistry</subject><subject>Biological and Medical Physics</subject><subject>Biomedical and Life Sciences</subject><subject>Biophysics</subject><subject>Cell Biology</subject><subject>Dimyristoylphosphatidylcholine - chemistry</subject><subject>Interferometry</subject><subject>Life Sciences</subject><subject>Lipid Bilayers - chemistry</subject><subject>Membrane Biology</subject><subject>Mode of action</subject><subject>Nanotechnology</subject><subject>Neurobiology</subject><subject>Original Paper</subject><subject>Peptides</subject><subject>Phosphatidylglycerols - chemistry</subject><subject>Static 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2
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| ispartof | European biophysics journal, 2013-01, Vol.42 (1), p.47-59 |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Amphibian Proteins - chemistry Antimicrobial Cationic Peptides - chemistry Biochemistry Biological and Medical Physics Biomedical and Life Sciences Biophysics Cell Biology Dimyristoylphosphatidylcholine - chemistry Interferometry Life Sciences Lipid Bilayers - chemistry Membrane Biology Mode of action Nanotechnology Neurobiology Original Paper Peptides Phosphatidylglycerols - chemistry Static Electricity |
| title | Structural effects of the antimicrobial peptide maculatin 1.1 on supported lipid bilayers |
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