Amphipathic Antimicrobial Piscidin in Magnetically Aligned Lipid Bilayers
The amphipathic antimicrobial peptide piscidin 1 was studied in magnetically aligned phospholipid bilayers by oriented-sample solid-state NMR spectroscopy. 31P NMR and double-resonance 1H/ 15N NMR experiments performed between 25°C and 61°C enabled the lipid headgroups as well as the peptide amide s...
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| Veröffentlicht in: | Biophysical journal 2011-09, Vol.101 (5), p.1086-1094 |
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| creator | De Angelis, Anna A. Grant, Christopher V. Baxter, Matthew K. McGavin, Jason A. Opella, Stanley J. Cotten, Myriam L. |
| description | The amphipathic antimicrobial peptide piscidin 1 was studied in magnetically aligned phospholipid bilayers by oriented-sample solid-state NMR spectroscopy.
31P NMR and double-resonance
1H/
15N NMR experiments performed between 25°C and 61°C enabled the lipid headgroups as well as the peptide amide sites to be monitored over a range of temperatures. The
α-helical peptide dramatically affects the phase behavior and structure of anionic bilayers but not those of zwitterionic bilayers. Piscidin 1 stabilizes anionic bilayers, which remain well aligned up to 61°C when piscidin 1 is on the membrane surface. Two-dimensional separated-local-field experiments show that the tilt angle of the peptide is 80 ± 5°, in agreement with previous results on mechanically aligned bilayers. The peptide undergoes fast rotational diffusion about the bilayer normal under these conditions, and these studies demonstrate that magnetically aligned bilayers are well suited for structural studies of amphipathic peptides. |
| doi_str_mv | 10.1016/j.bpj.2011.07.015 |
| format | Article |
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31P NMR and double-resonance
1H/
15N NMR experiments performed between 25°C and 61°C enabled the lipid headgroups as well as the peptide amide sites to be monitored over a range of temperatures. The
α-helical peptide dramatically affects the phase behavior and structure of anionic bilayers but not those of zwitterionic bilayers. Piscidin 1 stabilizes anionic bilayers, which remain well aligned up to 61°C when piscidin 1 is on the membrane surface. Two-dimensional separated-local-field experiments show that the tilt angle of the peptide is 80 ± 5°, in agreement with previous results on mechanically aligned bilayers. The peptide undergoes fast rotational diffusion about the bilayer normal under these conditions, and these studies demonstrate that magnetically aligned bilayers are well suited for structural studies of amphipathic peptides.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/j.bpj.2011.07.015</identifier><identifier>PMID: 21889445</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Antimicrobial agents ; Antimicrobial Cationic Peptides - chemistry ; Antimicrobial Cationic Peptides - metabolism ; antimicrobial peptides ; Feasibility Studies ; Fish Proteins - chemistry ; Fish Proteins - metabolism ; Hydrophobic and Hydrophilic Interactions ; lipid bilayers ; Lipid Bilayers - chemistry ; Lipid Bilayers - metabolism ; Magnetic Phenomena ; Magnetic Resonance Spectroscopy ; Membrane ; Molecular Sequence Data ; NMR ; Nuclear magnetic resonance ; nuclear magnetic resonance spectroscopy ; Peptides ; phospholipids ; Protein Structure, Secondary ; Proteins ; Spectrum analysis ; Temperature ; zwitterions</subject><ispartof>Biophysical journal, 2011-09, Vol.101 (5), p.1086-1094</ispartof><rights>2011 Biophysical Society</rights><rights>Copyright © 2011 Biophysical Society. Published by Elsevier Inc. All rights reserved.</rights><rights>Copyright Biophysical Society Sep 7, 2011</rights><rights>2011 by the Biophysical Society. 2011 Biophysical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c534t-68fa088b194d56de6b4912c27f58351f130a3d97022d0e4f32150ba974dfcc9a3</citedby><cites>FETCH-LOGICAL-c534t-68fa088b194d56de6b4912c27f58351f130a3d97022d0e4f32150ba974dfcc9a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3164131/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006349511008459$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,3537,27901,27902,53766,53768,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21889445$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>De Angelis, Anna A.</creatorcontrib><creatorcontrib>Grant, Christopher V.</creatorcontrib><creatorcontrib>Baxter, Matthew K.</creatorcontrib><creatorcontrib>McGavin, Jason A.</creatorcontrib><creatorcontrib>Opella, Stanley J.</creatorcontrib><creatorcontrib>Cotten, Myriam L.</creatorcontrib><title>Amphipathic Antimicrobial Piscidin in Magnetically Aligned Lipid Bilayers</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>The amphipathic antimicrobial peptide piscidin 1 was studied in magnetically aligned phospholipid bilayers by oriented-sample solid-state NMR spectroscopy.
31P NMR and double-resonance
1H/
15N NMR experiments performed between 25°C and 61°C enabled the lipid headgroups as well as the peptide amide sites to be monitored over a range of temperatures. The
α-helical peptide dramatically affects the phase behavior and structure of anionic bilayers but not those of zwitterionic bilayers. Piscidin 1 stabilizes anionic bilayers, which remain well aligned up to 61°C when piscidin 1 is on the membrane surface. Two-dimensional separated-local-field experiments show that the tilt angle of the peptide is 80 ± 5°, in agreement with previous results on mechanically aligned bilayers. The peptide undergoes fast rotational diffusion about the bilayer normal under these conditions, and these studies demonstrate that magnetically aligned bilayers are well suited for structural studies of amphipathic peptides.</description><subject>Amino Acid Sequence</subject><subject>Antimicrobial agents</subject><subject>Antimicrobial Cationic Peptides - chemistry</subject><subject>Antimicrobial Cationic Peptides - metabolism</subject><subject>antimicrobial peptides</subject><subject>Feasibility Studies</subject><subject>Fish Proteins - chemistry</subject><subject>Fish Proteins - metabolism</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>lipid bilayers</subject><subject>Lipid Bilayers - chemistry</subject><subject>Lipid Bilayers - metabolism</subject><subject>Magnetic Phenomena</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Membrane</subject><subject>Molecular Sequence Data</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>nuclear magnetic resonance spectroscopy</subject><subject>Peptides</subject><subject>phospholipids</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Spectrum analysis</subject><subject>Temperature</subject><subject>zwitterions</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kV2L1DAUhoMo7rj6A7zR4o3etObko00RhHHxY2FEQfc6pEk6c0qnrWlnYf69Z5l1US8WAoeQJy_nnIex58AL4FC-7Ypm6grBAQpeFRz0A7YCrUTOuSkfshXnvMylqvUZezLPHecgNIfH7EyAMbVSesUu1_tph5Nbduiz9bDgHn0aG3R99h1njwGHjM5Xtx3igt71_TFb90i3kG1wwpB9wN4dY5qfsket6-f47Laes6tPH39efMk33z5fXqw3uddSLXlpWseNaaBWQZchlo2qQXhRtdpIDS1I7mSoKy5E4FG1UoDmjasrFVrvayfP2ftT7nRo9jH4OCzJ9XZKuHfpaEeH9t-XAXd2O15bCaUCCRTw-jYgjb8OcV7sniaNfe-GOB5ma0xVaSNESeSbe0kQAkBKaQShr_5Du_GQBloE5dWiNEZJguAE0YrnOcX2rmvg9sao7SwZtTdGLa8sGaU_L_4e9-7HH4UEvDwBrRut2yac7dUPStCkG6jWRLw7EZG0XGNMlsTGwceAKfrFhhHvaeA3SNC5jg</recordid><startdate>20110907</startdate><enddate>20110907</enddate><creator>De Angelis, Anna A.</creator><creator>Grant, Christopher V.</creator><creator>Baxter, Matthew K.</creator><creator>McGavin, Jason A.</creator><creator>Opella, Stanley J.</creator><creator>Cotten, Myriam L.</creator><general>Elsevier Inc</general><general>Biophysical Society</general><general>The Biophysical Society</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>7T7</scope><scope>C1K</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20110907</creationdate><title>Amphipathic Antimicrobial Piscidin in Magnetically Aligned Lipid Bilayers</title><author>De Angelis, Anna A. ; Grant, Christopher V. ; Baxter, Matthew K. ; McGavin, Jason A. ; Opella, Stanley J. ; Cotten, Myriam L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c534t-68fa088b194d56de6b4912c27f58351f130a3d97022d0e4f32150ba974dfcc9a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino Acid Sequence</topic><topic>Antimicrobial agents</topic><topic>Antimicrobial Cationic Peptides - chemistry</topic><topic>Antimicrobial Cationic Peptides - metabolism</topic><topic>antimicrobial peptides</topic><topic>Feasibility Studies</topic><topic>Fish Proteins - chemistry</topic><topic>Fish Proteins - metabolism</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>lipid bilayers</topic><topic>Lipid Bilayers - chemistry</topic><topic>Lipid Bilayers - metabolism</topic><topic>Magnetic Phenomena</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Membrane</topic><topic>Molecular Sequence Data</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><topic>nuclear magnetic resonance spectroscopy</topic><topic>Peptides</topic><topic>phospholipids</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Spectrum analysis</topic><topic>Temperature</topic><topic>zwitterions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>De Angelis, Anna A.</creatorcontrib><creatorcontrib>Grant, Christopher V.</creatorcontrib><creatorcontrib>Baxter, Matthew K.</creatorcontrib><creatorcontrib>McGavin, Jason A.</creatorcontrib><creatorcontrib>Opella, Stanley J.</creatorcontrib><creatorcontrib>Cotten, Myriam L.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>De Angelis, Anna A.</au><au>Grant, Christopher V.</au><au>Baxter, Matthew K.</au><au>McGavin, Jason A.</au><au>Opella, Stanley J.</au><au>Cotten, Myriam L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amphipathic Antimicrobial Piscidin in Magnetically Aligned Lipid Bilayers</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>2011-09-07</date><risdate>2011</risdate><volume>101</volume><issue>5</issue><spage>1086</spage><epage>1094</epage><pages>1086-1094</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>The amphipathic antimicrobial peptide piscidin 1 was studied in magnetically aligned phospholipid bilayers by oriented-sample solid-state NMR spectroscopy.
31P NMR and double-resonance
1H/
15N NMR experiments performed between 25°C and 61°C enabled the lipid headgroups as well as the peptide amide sites to be monitored over a range of temperatures. The
α-helical peptide dramatically affects the phase behavior and structure of anionic bilayers but not those of zwitterionic bilayers. Piscidin 1 stabilizes anionic bilayers, which remain well aligned up to 61°C when piscidin 1 is on the membrane surface. Two-dimensional separated-local-field experiments show that the tilt angle of the peptide is 80 ± 5°, in agreement with previous results on mechanically aligned bilayers. The peptide undergoes fast rotational diffusion about the bilayer normal under these conditions, and these studies demonstrate that magnetically aligned bilayers are well suited for structural studies of amphipathic peptides.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>21889445</pmid><doi>10.1016/j.bpj.2011.07.015</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Amino Acid Sequence Antimicrobial agents Antimicrobial Cationic Peptides - chemistry Antimicrobial Cationic Peptides - metabolism antimicrobial peptides Feasibility Studies Fish Proteins - chemistry Fish Proteins - metabolism Hydrophobic and Hydrophilic Interactions lipid bilayers Lipid Bilayers - chemistry Lipid Bilayers - metabolism Magnetic Phenomena Magnetic Resonance Spectroscopy Membrane Molecular Sequence Data NMR Nuclear magnetic resonance nuclear magnetic resonance spectroscopy Peptides phospholipids Protein Structure, Secondary Proteins Spectrum analysis Temperature zwitterions |
| title | Amphipathic Antimicrobial Piscidin in Magnetically Aligned Lipid Bilayers |
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