Coupling of spectrin and polylysine to phospholipid monolayers studied by specular reflection of neutrons
The technique of specular reflection of neutrons is applied for the first time to study the charge-dependent interaction of the protein spectrin and the polypeptide poly-L-lysine with model phospholipid monolayers in the condensed phase state. We first established the structure of a pure monolayer o...
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| Veröffentlicht in: | Biophysical journal 1991-11, Vol.60 (5), p.1017-1025 |
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| container_title | Biophysical journal |
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| creator | Johnson, S.J. Bayerl, T.M. Weihan, W. Noack, H. Penfold, J. Thomas, R.K. Kanellas, D. Rennie, A.R. Sackmann, E. |
| description | The technique of specular reflection of neutrons is applied for the first time to study the charge-dependent interaction of the protein spectrin and the polypeptide poly-L-lysine with model phospholipid monolayers in the condensed phase state. We first established the structure of a pure monolayer of dimyristolyphosphatidylcholine (DMPC) in both the expanded and condensed fluid phase states without protein in the subphase. The thickness of the hydrocarbon chains increases from 11.4 +/- 1.5 A in the expanded state to 15.8 +/- 1.5 A in the condensed state, whereas the head group region is approximately 10 A thick for both phase states. When spectrin is present in the subphase, the dimensions of DMPC in the condensed state are not significantly affected, but there is approximately 0.09 volume fraction spectrin in the head group region. Lipid-spectrin coupling is enhanced by electrostatic interaction, as the volume fraction of spectrin in the head group region increases to 0.22 in a mixed monolayer of DMPC and negatively charged dimyristolyphosphatidylglycerol in the condensed state. In contrast to spectrin, polylysine does not penetrate the head group region, but forms a layer electrostatically adsorbed to the charged head groups. |
| doi_str_mv | 10.1016/S0006-3495(91)82139-7 |
| format | Article |
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We first established the structure of a pure monolayer of dimyristolyphosphatidylcholine (DMPC) in both the expanded and condensed fluid phase states without protein in the subphase. The thickness of the hydrocarbon chains increases from 11.4 +/- 1.5 A in the expanded state to 15.8 +/- 1.5 A in the condensed state, whereas the head group region is approximately 10 A thick for both phase states. When spectrin is present in the subphase, the dimensions of DMPC in the condensed state are not significantly affected, but there is approximately 0.09 volume fraction spectrin in the head group region. Lipid-spectrin coupling is enhanced by electrostatic interaction, as the volume fraction of spectrin in the head group region increases to 0.22 in a mixed monolayer of DMPC and negatively charged dimyristolyphosphatidylglycerol in the condensed state. In contrast to spectrin, polylysine does not penetrate the head group region, but forms a layer electrostatically adsorbed to the charged head groups.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(91)82139-7</identifier><identifier>PMID: 1760501</identifier><identifier>CODEN: BIOJAU</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Artificial membranes and reconstituted systems ; Biological and medical sciences ; Biophysical Phenomena ; Biophysics ; Dimyristoylphosphatidylcholine - chemistry ; Electrochemistry ; Fundamental and applied biological sciences. Psychology ; Membrane physicochemistry ; Models, Chemical ; Molecular biophysics ; Molecular Structure ; Neutrons ; Phosphatidylglycerols - chemistry ; Phospholipids - chemistry ; polylysine ; Polylysine - chemistry ; Scattering, Radiation ; spectrin ; Spectrin - chemistry</subject><ispartof>Biophysical journal, 1991-11, Vol.60 (5), p.1017-1025</ispartof><rights>1991 The Biophysical Society</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c522t-7fb6b298471143bf29e5a51340cc0c5f004e94f54b143f2f7be16199902051033</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1260159/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-3495(91)82139-7$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,3550,27924,27925,45995,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5063040$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1760501$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Johnson, S.J.</creatorcontrib><creatorcontrib>Bayerl, T.M.</creatorcontrib><creatorcontrib>Weihan, W.</creatorcontrib><creatorcontrib>Noack, H.</creatorcontrib><creatorcontrib>Penfold, J.</creatorcontrib><creatorcontrib>Thomas, R.K.</creatorcontrib><creatorcontrib>Kanellas, D.</creatorcontrib><creatorcontrib>Rennie, A.R.</creatorcontrib><creatorcontrib>Sackmann, E.</creatorcontrib><title>Coupling of spectrin and polylysine to phospholipid monolayers studied by specular reflection of neutrons</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>The technique of specular reflection of neutrons is applied for the first time to study the charge-dependent interaction of the protein spectrin and the polypeptide poly-L-lysine with model phospholipid monolayers in the condensed phase state. We first established the structure of a pure monolayer of dimyristolyphosphatidylcholine (DMPC) in both the expanded and condensed fluid phase states without protein in the subphase. The thickness of the hydrocarbon chains increases from 11.4 +/- 1.5 A in the expanded state to 15.8 +/- 1.5 A in the condensed state, whereas the head group region is approximately 10 A thick for both phase states. When spectrin is present in the subphase, the dimensions of DMPC in the condensed state are not significantly affected, but there is approximately 0.09 volume fraction spectrin in the head group region. Lipid-spectrin coupling is enhanced by electrostatic interaction, as the volume fraction of spectrin in the head group region increases to 0.22 in a mixed monolayer of DMPC and negatively charged dimyristolyphosphatidylglycerol in the condensed state. In contrast to spectrin, polylysine does not penetrate the head group region, but forms a layer electrostatically adsorbed to the charged head groups.</description><subject>Artificial membranes and reconstituted systems</subject><subject>Biological and medical sciences</subject><subject>Biophysical Phenomena</subject><subject>Biophysics</subject><subject>Dimyristoylphosphatidylcholine - chemistry</subject><subject>Electrochemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Membrane physicochemistry</subject><subject>Models, Chemical</subject><subject>Molecular biophysics</subject><subject>Molecular Structure</subject><subject>Neutrons</subject><subject>Phosphatidylglycerols - chemistry</subject><subject>Phospholipids - chemistry</subject><subject>polylysine</subject><subject>Polylysine - chemistry</subject><subject>Scattering, Radiation</subject><subject>spectrin</subject><subject>Spectrin - chemistry</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUuPFCEUhYnRjO3oT5iEhTG6KL1QQBUbJ6bjK5nEhbomFAUzGBpKqJqk_r30I62uZkEgOd89OdyD0BWBtwSIePcdAETTMslfS_Kmp6SVTfcIbQhntAHoxWO0OSNP0bNSfgEQyoFcoAvSCaivDfLbtEzBx1ucHC6TNXP2Ees44imFNazFR4vnhKe7VOoJfvIj3qWYgl5tLrjMy-jtiIf1ML0EnXG2LlQjn-LeNNplzimW5-iJ06HYF6f7Ev389PHH9ktz8-3z1-2Hm8ZwSuemc4MYqOxZRwhrB0el5ZqTloExYLgDYFYyx9lQZUddN1giiJQSKHACbXuJ3h99p2XY2dHYOGcd1JT9TudVJe3V_0r0d-o23StCBRAuq8Grk0FOvxdbZrXzxdgQdLRpKaqjXHDWPwzWXH2NRSvIj6DJqZS6nnMaAmpfpjqUqfZNKUnUoUzV1bmrf7_yd-rYXtVfnnRdjA4u62h8OWMcRAsMKnZ9xGxd-723WRXjbTR29Ln2pMbkHwjyB4-MvYE</recordid><startdate>19911101</startdate><enddate>19911101</enddate><creator>Johnson, S.J.</creator><creator>Bayerl, T.M.</creator><creator>Weihan, W.</creator><creator>Noack, H.</creator><creator>Penfold, J.</creator><creator>Thomas, R.K.</creator><creator>Kanellas, D.</creator><creator>Rennie, A.R.</creator><creator>Sackmann, E.</creator><general>Elsevier Inc</general><general>Biophysical Society</general><scope>6I.</scope><scope>AAFTH</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19911101</creationdate><title>Coupling of spectrin and polylysine to phospholipid monolayers studied by specular reflection of neutrons</title><author>Johnson, S.J. ; Bayerl, T.M. ; Weihan, W. ; Noack, H. ; Penfold, J. ; Thomas, R.K. ; Kanellas, D. ; Rennie, A.R. ; Sackmann, E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c522t-7fb6b298471143bf29e5a51340cc0c5f004e94f54b143f2f7be16199902051033</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Artificial membranes and reconstituted systems</topic><topic>Biological and medical sciences</topic><topic>Biophysical Phenomena</topic><topic>Biophysics</topic><topic>Dimyristoylphosphatidylcholine - chemistry</topic><topic>Electrochemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Membrane physicochemistry</topic><topic>Models, Chemical</topic><topic>Molecular biophysics</topic><topic>Molecular Structure</topic><topic>Neutrons</topic><topic>Phosphatidylglycerols - chemistry</topic><topic>Phospholipids - chemistry</topic><topic>polylysine</topic><topic>Polylysine - chemistry</topic><topic>Scattering, Radiation</topic><topic>spectrin</topic><topic>Spectrin - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Johnson, S.J.</creatorcontrib><creatorcontrib>Bayerl, T.M.</creatorcontrib><creatorcontrib>Weihan, W.</creatorcontrib><creatorcontrib>Noack, H.</creatorcontrib><creatorcontrib>Penfold, J.</creatorcontrib><creatorcontrib>Thomas, R.K.</creatorcontrib><creatorcontrib>Kanellas, D.</creatorcontrib><creatorcontrib>Rennie, A.R.</creatorcontrib><creatorcontrib>Sackmann, E.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</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>Johnson, S.J.</au><au>Bayerl, T.M.</au><au>Weihan, W.</au><au>Noack, H.</au><au>Penfold, J.</au><au>Thomas, R.K.</au><au>Kanellas, D.</au><au>Rennie, A.R.</au><au>Sackmann, E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Coupling of spectrin and polylysine to phospholipid monolayers studied by specular reflection of neutrons</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1991-11-01</date><risdate>1991</risdate><volume>60</volume><issue>5</issue><spage>1017</spage><epage>1025</epage><pages>1017-1025</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><coden>BIOJAU</coden><abstract>The technique of specular reflection of neutrons is applied for the first time to study the charge-dependent interaction of the protein spectrin and the polypeptide poly-L-lysine with model phospholipid monolayers in the condensed phase state. We first established the structure of a pure monolayer of dimyristolyphosphatidylcholine (DMPC) in both the expanded and condensed fluid phase states without protein in the subphase. The thickness of the hydrocarbon chains increases from 11.4 +/- 1.5 A in the expanded state to 15.8 +/- 1.5 A in the condensed state, whereas the head group region is approximately 10 A thick for both phase states. When spectrin is present in the subphase, the dimensions of DMPC in the condensed state are not significantly affected, but there is approximately 0.09 volume fraction spectrin in the head group region. Lipid-spectrin coupling is enhanced by electrostatic interaction, as the volume fraction of spectrin in the head group region increases to 0.22 in a mixed monolayer of DMPC and negatively charged dimyristolyphosphatidylglycerol in the condensed state. In contrast to spectrin, polylysine does not penetrate the head group region, but forms a layer electrostatically adsorbed to the charged head groups.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>1760501</pmid><doi>10.1016/S0006-3495(91)82139-7</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biophysical journal, 1991-11, Vol.60 (5), p.1017-1025 |
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| language | eng |
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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Artificial membranes and reconstituted systems Biological and medical sciences Biophysical Phenomena Biophysics Dimyristoylphosphatidylcholine - chemistry Electrochemistry Fundamental and applied biological sciences. Psychology Membrane physicochemistry Models, Chemical Molecular biophysics Molecular Structure Neutrons Phosphatidylglycerols - chemistry Phospholipids - chemistry polylysine Polylysine - chemistry Scattering, Radiation spectrin Spectrin - chemistry |
| title | Coupling of spectrin and polylysine to phospholipid monolayers studied by specular reflection of neutrons |
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