NMR Structure and Dynamic Studies of an Anion-Binding, Channel-Forming Heptapeptide
The synthetic peptide (C18H37)2NCOCH2OCH2CON−(Gly)3−Pro−(Gly)3−OCH2Ph forms chloride-selective channels in liposomes and exhibits voltage-gating properties in planar phospholipid bilayers. The peptide fragment of the channel is based on a conserved motif in naturally occurring chloride transporters....
Gespeichert in:
| Veröffentlicht in: | Journal of the American Chemical Society 2006-02, Vol.128 (5), p.1633-1638 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1638 |
|---|---|
| container_issue | 5 |
| container_start_page | 1633 |
| container_title | Journal of the American Chemical Society |
| container_volume | 128 |
| creator | Cook, Gabriel A Pajewski, Robert Aburi, Mahalaxmi Smith, Paul E Prakash, Om Tomich, John M Gokel, George W |
| description | The synthetic peptide (C18H37)2NCOCH2OCH2CON−(Gly)3−Pro−(Gly)3−OCH2Ph forms chloride-selective channels in liposomes and exhibits voltage-gating properties in planar phospholipid bilayers. The peptide fragment of the channel is based on a conserved motif in naturally occurring chloride transporters. Membrane-anchoring residues at the N- and C-terminal ends augment the peptide. NMR spectra (1D and 2D) of the channel in CDCl3 showed significant variation in the absence and presence of stoichiometric tetrabutylammonium chloride (Bu4NCl). One-dimensional solution-state NMR titration studies combined with computational molecular simulation studies indicate that the peptide interacts with the salt as an ion pair and H-bonds chloride. To our knowledge, this is the first structural analysis of any synthetic anion-channel salt complex. |
| doi_str_mv | 10.1021/ja055887j |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_70719964</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>70719964</sourcerecordid><originalsourceid>FETCH-LOGICAL-a381t-ff59782bcbe457ae4e7271ffda44efb0b8e35d58fc1ad8068ebcbc7a4aa001093</originalsourceid><addsrcrecordid>eNpt0M1u3CAUBWBUNWomaRd5gcibVooUt2CDYZbp5F-TtqrTNbrGl4SpjSdgS83bh2hGmU03IA6fLugQcsToV0YL9m0FVAil5OodmTFR0FywonpPZpTSIpeqKvfJQYyrdOSFYh_IPqs4V6ysZqT-cfc7q8cwmXEKmIFvs_NnD70zKZ1ahzEbbIqzM-8Gn393vnX-4TRbPIL32OWXQ-hTkF3jeoR1WlyLH8mehS7ip-1-SP5cXtwvrvPlz6ubxdkyh1KxMbdWzKUqGtMgFxKQoywks7YFztE2tFFYilYoaxi0ilYKEzUSOACljM7LQ_JlM3cdhqcJ46h7Fw12HXgcpqgllWw-r3iCJxtowhBjQKvXwfUQnjWj-rVB_dZgssfboVPTY7uT28oS-LwFEA10NoA3Lu6cTI8q8eryjXNxxH9v9xD-6kqWUuj7X7Uu7upzUS9LfbubCybq1TAFn7r7zwdfAHbdk6c</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>70719964</pqid></control><display><type>article</type><title>NMR Structure and Dynamic Studies of an Anion-Binding, Channel-Forming Heptapeptide</title><source>MEDLINE</source><source>American Chemical Society Journals</source><creator>Cook, Gabriel A ; Pajewski, Robert ; Aburi, Mahalaxmi ; Smith, Paul E ; Prakash, Om ; Tomich, John M ; Gokel, George W</creator><creatorcontrib>Cook, Gabriel A ; Pajewski, Robert ; Aburi, Mahalaxmi ; Smith, Paul E ; Prakash, Om ; Tomich, John M ; Gokel, George W</creatorcontrib><description>The synthetic peptide (C18H37)2NCOCH2OCH2CON−(Gly)3−Pro−(Gly)3−OCH2Ph forms chloride-selective channels in liposomes and exhibits voltage-gating properties in planar phospholipid bilayers. The peptide fragment of the channel is based on a conserved motif in naturally occurring chloride transporters. Membrane-anchoring residues at the N- and C-terminal ends augment the peptide. NMR spectra (1D and 2D) of the channel in CDCl3 showed significant variation in the absence and presence of stoichiometric tetrabutylammonium chloride (Bu4NCl). One-dimensional solution-state NMR titration studies combined with computational molecular simulation studies indicate that the peptide interacts with the salt as an ion pair and H-bonds chloride. To our knowledge, this is the first structural analysis of any synthetic anion-channel salt complex.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja055887j</identifier><identifier>PMID: 16448136</identifier><identifier>CODEN: JACSAT</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Biological and medical sciences ; Chemistry ; Chloride Channels - chemistry ; Chloride Channels - metabolism ; Circular Dichroism ; Computer Simulation ; Exact sciences and technology ; Fundamental and applied biological sciences. Psychology ; General and physical chemistry ; In solution. Condensed state. Thin layers ; Lipid Bilayers - chemistry ; Lipid Bilayers - metabolism ; Liposomes - chemistry ; Models, Molecular ; Molecular biophysics ; Nuclear Magnetic Resonance, Biomolecular - methods ; Oligopeptides - chemical synthesis ; Oligopeptides - chemistry ; Oligopeptides - metabolism ; Physico-chemical properties of biomolecules ; Protein Conformation ; Solution properties ; Solutions</subject><ispartof>Journal of the American Chemical Society, 2006-02, Vol.128 (5), p.1633-1638</ispartof><rights>Copyright © 2006 American Chemical Society</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a381t-ff59782bcbe457ae4e7271ffda44efb0b8e35d58fc1ad8068ebcbc7a4aa001093</citedby><cites>FETCH-LOGICAL-a381t-ff59782bcbe457ae4e7271ffda44efb0b8e35d58fc1ad8068ebcbc7a4aa001093</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/ja055887j$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ja055887j$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2763,27075,27923,27924,56737,56787</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17719856$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16448136$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cook, Gabriel A</creatorcontrib><creatorcontrib>Pajewski, Robert</creatorcontrib><creatorcontrib>Aburi, Mahalaxmi</creatorcontrib><creatorcontrib>Smith, Paul E</creatorcontrib><creatorcontrib>Prakash, Om</creatorcontrib><creatorcontrib>Tomich, John M</creatorcontrib><creatorcontrib>Gokel, George W</creatorcontrib><title>NMR Structure and Dynamic Studies of an Anion-Binding, Channel-Forming Heptapeptide</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>The synthetic peptide (C18H37)2NCOCH2OCH2CON−(Gly)3−Pro−(Gly)3−OCH2Ph forms chloride-selective channels in liposomes and exhibits voltage-gating properties in planar phospholipid bilayers. The peptide fragment of the channel is based on a conserved motif in naturally occurring chloride transporters. Membrane-anchoring residues at the N- and C-terminal ends augment the peptide. NMR spectra (1D and 2D) of the channel in CDCl3 showed significant variation in the absence and presence of stoichiometric tetrabutylammonium chloride (Bu4NCl). One-dimensional solution-state NMR titration studies combined with computational molecular simulation studies indicate that the peptide interacts with the salt as an ion pair and H-bonds chloride. To our knowledge, this is the first structural analysis of any synthetic anion-channel salt complex.</description><subject>Biological and medical sciences</subject><subject>Chemistry</subject><subject>Chloride Channels - chemistry</subject><subject>Chloride Channels - metabolism</subject><subject>Circular Dichroism</subject><subject>Computer Simulation</subject><subject>Exact sciences and technology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General and physical chemistry</subject><subject>In solution. Condensed state. Thin layers</subject><subject>Lipid Bilayers - chemistry</subject><subject>Lipid Bilayers - metabolism</subject><subject>Liposomes - chemistry</subject><subject>Models, Molecular</subject><subject>Molecular biophysics</subject><subject>Nuclear Magnetic Resonance, Biomolecular - methods</subject><subject>Oligopeptides - chemical synthesis</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - metabolism</subject><subject>Physico-chemical properties of biomolecules</subject><subject>Protein Conformation</subject><subject>Solution properties</subject><subject>Solutions</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0M1u3CAUBWBUNWomaRd5gcibVooUt2CDYZbp5F-TtqrTNbrGl4SpjSdgS83bh2hGmU03IA6fLugQcsToV0YL9m0FVAil5OodmTFR0FywonpPZpTSIpeqKvfJQYyrdOSFYh_IPqs4V6ysZqT-cfc7q8cwmXEKmIFvs_NnD70zKZ1ahzEbbIqzM-8Gn393vnX-4TRbPIL32OWXQ-hTkF3jeoR1WlyLH8mehS7ip-1-SP5cXtwvrvPlz6ubxdkyh1KxMbdWzKUqGtMgFxKQoywks7YFztE2tFFYilYoaxi0ilYKEzUSOACljM7LQ_JlM3cdhqcJ46h7Fw12HXgcpqgllWw-r3iCJxtowhBjQKvXwfUQnjWj-rVB_dZgssfboVPTY7uT28oS-LwFEA10NoA3Lu6cTI8q8eryjXNxxH9v9xD-6kqWUuj7X7Uu7upzUS9LfbubCybq1TAFn7r7zwdfAHbdk6c</recordid><startdate>20060208</startdate><enddate>20060208</enddate><creator>Cook, Gabriel A</creator><creator>Pajewski, Robert</creator><creator>Aburi, Mahalaxmi</creator><creator>Smith, Paul E</creator><creator>Prakash, Om</creator><creator>Tomich, John M</creator><creator>Gokel, George W</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</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>7X8</scope></search><sort><creationdate>20060208</creationdate><title>NMR Structure and Dynamic Studies of an Anion-Binding, Channel-Forming Heptapeptide</title><author>Cook, Gabriel A ; Pajewski, Robert ; Aburi, Mahalaxmi ; Smith, Paul E ; Prakash, Om ; Tomich, John M ; Gokel, George W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a381t-ff59782bcbe457ae4e7271ffda44efb0b8e35d58fc1ad8068ebcbc7a4aa001093</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Biological and medical sciences</topic><topic>Chemistry</topic><topic>Chloride Channels - chemistry</topic><topic>Chloride Channels - metabolism</topic><topic>Circular Dichroism</topic><topic>Computer Simulation</topic><topic>Exact sciences and technology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General and physical chemistry</topic><topic>In solution. Condensed state. Thin layers</topic><topic>Lipid Bilayers - chemistry</topic><topic>Lipid Bilayers - metabolism</topic><topic>Liposomes - chemistry</topic><topic>Models, Molecular</topic><topic>Molecular biophysics</topic><topic>Nuclear Magnetic Resonance, Biomolecular - methods</topic><topic>Oligopeptides - chemical synthesis</topic><topic>Oligopeptides - chemistry</topic><topic>Oligopeptides - metabolism</topic><topic>Physico-chemical properties of biomolecules</topic><topic>Protein Conformation</topic><topic>Solution properties</topic><topic>Solutions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cook, Gabriel A</creatorcontrib><creatorcontrib>Pajewski, Robert</creatorcontrib><creatorcontrib>Aburi, Mahalaxmi</creatorcontrib><creatorcontrib>Smith, Paul E</creatorcontrib><creatorcontrib>Prakash, Om</creatorcontrib><creatorcontrib>Tomich, John M</creatorcontrib><creatorcontrib>Gokel, George W</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cook, Gabriel A</au><au>Pajewski, Robert</au><au>Aburi, Mahalaxmi</au><au>Smith, Paul E</au><au>Prakash, Om</au><au>Tomich, John M</au><au>Gokel, George W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>NMR Structure and Dynamic Studies of an Anion-Binding, Channel-Forming Heptapeptide</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2006-02-08</date><risdate>2006</risdate><volume>128</volume><issue>5</issue><spage>1633</spage><epage>1638</epage><pages>1633-1638</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>The synthetic peptide (C18H37)2NCOCH2OCH2CON−(Gly)3−Pro−(Gly)3−OCH2Ph forms chloride-selective channels in liposomes and exhibits voltage-gating properties in planar phospholipid bilayers. The peptide fragment of the channel is based on a conserved motif in naturally occurring chloride transporters. Membrane-anchoring residues at the N- and C-terminal ends augment the peptide. NMR spectra (1D and 2D) of the channel in CDCl3 showed significant variation in the absence and presence of stoichiometric tetrabutylammonium chloride (Bu4NCl). One-dimensional solution-state NMR titration studies combined with computational molecular simulation studies indicate that the peptide interacts with the salt as an ion pair and H-bonds chloride. To our knowledge, this is the first structural analysis of any synthetic anion-channel salt complex.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>16448136</pmid><doi>10.1021/ja055887j</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0002-7863 |
| ispartof | Journal of the American Chemical Society, 2006-02, Vol.128 (5), p.1633-1638 |
| issn | 0002-7863 1520-5126 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70719964 |
| source | MEDLINE; American Chemical Society Journals |
| subjects | Biological and medical sciences Chemistry Chloride Channels - chemistry Chloride Channels - metabolism Circular Dichroism Computer Simulation Exact sciences and technology Fundamental and applied biological sciences. Psychology General and physical chemistry In solution. Condensed state. Thin layers Lipid Bilayers - chemistry Lipid Bilayers - metabolism Liposomes - chemistry Models, Molecular Molecular biophysics Nuclear Magnetic Resonance, Biomolecular - methods Oligopeptides - chemical synthesis Oligopeptides - chemistry Oligopeptides - metabolism Physico-chemical properties of biomolecules Protein Conformation Solution properties Solutions |
| title | NMR Structure and Dynamic Studies of an Anion-Binding, Channel-Forming Heptapeptide |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-13T01%3A21%3A08IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=NMR%20Structure%20and%20Dynamic%20Studies%20of%20an%20Anion-Binding,%20Channel-Forming%20Heptapeptide&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.au=Cook,%20Gabriel%20A&rft.date=2006-02-08&rft.volume=128&rft.issue=5&rft.spage=1633&rft.epage=1638&rft.pages=1633-1638&rft.issn=0002-7863&rft.eissn=1520-5126&rft.coden=JACSAT&rft_id=info:doi/10.1021/ja055887j&rft_dat=%3Cproquest_cross%3E70719964%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=70719964&rft_id=info:pmid/16448136&rfr_iscdi=true |