The use of UV-visible spectroscopy for the determination of hydrophobic interactions between neuropeptides and membrane model systems
Ultraviolet‐visible spectroscopy has been used as a rapid method to evaluate the hydrophobia interactions between a series of cationic and zwitterionic neuropeptides and dipeptides with the hydrophobia core of two membrane model systems; sodium dodecyl sulfate and lysophosphatidylcholine micelles. I...
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Veröffentlicht in: | Biopolymers 1992-08, Vol.32 (8), p.1061-1064 |
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description | Ultraviolet‐visible spectroscopy has been used as a rapid method to evaluate the hydrophobia interactions between a series of cationic and zwitterionic neuropeptides and dipeptides with the hydrophobia core of two membrane model systems; sodium dodecyl sulfate and lysophosphatidylcholine micelles. If a hydrophobia interaction occurs, a 1−nm bathochromic shift is observed in the uv‐visible spectrum of the aromatic side chains when going from aqueous solution to a micellar solution. The aromatic residues of substance P, bradykinin, and Des‐Arg9 bradykinin all exhibited the 1−nm bathochromic shift in the presence of sodium dodecyl sulfate while those of Met‐enkephalin did not. The opposite effects were observed in the presence of lysophosphatidylcholine micelles. © 1992 John Wiley & Sons, Inc. |
doi_str_mv | 10.1002/bip.360320815 |
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If a hydrophobia interaction occurs, a 1−nm bathochromic shift is observed in the uv‐visible spectrum of the aromatic side chains when going from aqueous solution to a micellar solution. The aromatic residues of substance P, bradykinin, and Des‐Arg9 bradykinin all exhibited the 1−nm bathochromic shift in the presence of sodium dodecyl sulfate while those of Met‐enkephalin did not. The opposite effects were observed in the presence of lysophosphatidylcholine micelles. © 1992 John Wiley & Sons, Inc.</description><identifier>ISSN: 0006-3525</identifier><identifier>EISSN: 1097-0282</identifier><identifier>DOI: 10.1002/bip.360320815</identifier><identifier>PMID: 1420972</identifier><identifier>CODEN: BIPMAA</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Amino Acid Sequence ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; hydrophobicity ; Interactions. Associations ; Intermolecular phenomena ; Lysophosphatidylcholines ; membranes ; Membranes - chemistry ; Membranes - metabolism ; Micelles ; Models, Biological ; Molecular biophysics ; Molecular Sequence Data ; neuropeptides ; Neuropeptides - chemistry ; Neuropeptides - metabolism ; Sodium Dodecyl Sulfate ; Spectrophotometry, Ultraviolet ; spectroscopy ; U.V. radiation ; Water - chemistry</subject><ispartof>Biopolymers, 1992-08, Vol.32 (8), p.1061-1064</ispartof><rights>Copyright © 1992 John Wiley & Sons, Inc.</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4345-3a0d6955ba1c4d7030cd5577982fc12b86a9be455f704b51cee5cf048ad956113</citedby><cites>FETCH-LOGICAL-c4345-3a0d6955ba1c4d7030cd5577982fc12b86a9be455f704b51cee5cf048ad956113</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbip.360320815$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbip.360320815$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5433578$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1420972$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Young, John K.</creatorcontrib><creatorcontrib>Graham, William H.</creatorcontrib><creatorcontrib>Beard, Debbie J.</creatorcontrib><creatorcontrib>Hicks, Rickey P.</creatorcontrib><title>The use of UV-visible spectroscopy for the determination of hydrophobic interactions between neuropeptides and membrane model systems</title><title>Biopolymers</title><addtitle>Biopolymers</addtitle><description>Ultraviolet‐visible spectroscopy has been used as a rapid method to evaluate the hydrophobia interactions between a series of cationic and zwitterionic neuropeptides and dipeptides with the hydrophobia core of two membrane model systems; sodium dodecyl sulfate and lysophosphatidylcholine micelles. If a hydrophobia interaction occurs, a 1−nm bathochromic shift is observed in the uv‐visible spectrum of the aromatic side chains when going from aqueous solution to a micellar solution. The aromatic residues of substance P, bradykinin, and Des‐Arg9 bradykinin all exhibited the 1−nm bathochromic shift in the presence of sodium dodecyl sulfate while those of Met‐enkephalin did not. The opposite effects were observed in the presence of lysophosphatidylcholine micelles. © 1992 John Wiley & Sons, Inc.</description><subject>Amino Acid Sequence</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hydrophobicity</subject><subject>Interactions. Associations</subject><subject>Intermolecular phenomena</subject><subject>Lysophosphatidylcholines</subject><subject>membranes</subject><subject>Membranes - chemistry</subject><subject>Membranes - metabolism</subject><subject>Micelles</subject><subject>Models, Biological</subject><subject>Molecular biophysics</subject><subject>Molecular Sequence Data</subject><subject>neuropeptides</subject><subject>Neuropeptides - chemistry</subject><subject>Neuropeptides - metabolism</subject><subject>Sodium Dodecyl Sulfate</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>spectroscopy</subject><subject>U.V. radiation</subject><subject>Water - chemistry</subject><issn>0006-3525</issn><issn>1097-0282</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUlvFDEQhS0ECkPgyBHJB8StQ3lrdx9hBCFSWCIlhJvlpVpj6I12N2F-AP8bj2Y0cIJTHd5XVU_vEfKUwRkD4C9dHM9ECYJDxdQ9smJQ6wJ4xe-TFQCUhVBcPSSPUvoKIKVgcEJOmOQZ4yvy63qDdElIh4befC5-xBRdizSN6OdpSH4Yt7QZJjpnLOCMUxd7O8eh3y1stmEaxs3goqexz6L1OylRh_MdYk97XDKA4xwDJmr7QDvs3GR7pN0QsKVpm2bs0mPyoLFtwieHeUpu3r65Xr8rLj-eX6xfXRZeCqkKYSGUtVLOMi-DBgE-KKV1XfHGM-6q0tYOpVKNBukU84jKNyArG2pVMiZOyYv93XEavi-YZtPF5LFts6NhSUYLXkMl-H9BVkpRg1YZLPagz2mlCRszTrGz09YwMLt-TO7HHPvJ_LPD4cV1GP7Q-0Ky_vyg2-Rt2-SsfExHTEkhlK4ypvfYXWxx---f5vXFp78NHAzHnPzP46advplSC63M7YdzI26rqy_vr0qzFr8BoAe53g</recordid><startdate>199208</startdate><enddate>199208</enddate><creator>Young, John K.</creator><creator>Graham, William H.</creator><creator>Beard, Debbie J.</creator><creator>Hicks, Rickey P.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley</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>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>199208</creationdate><title>The use of UV-visible spectroscopy for the determination of hydrophobic interactions between neuropeptides and membrane model systems</title><author>Young, John K. ; Graham, William H. ; Beard, Debbie J. ; Hicks, Rickey P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4345-3a0d6955ba1c4d7030cd5577982fc12b86a9be455f704b51cee5cf048ad956113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hydrophobicity</topic><topic>Interactions. Associations</topic><topic>Intermolecular phenomena</topic><topic>Lysophosphatidylcholines</topic><topic>membranes</topic><topic>Membranes - chemistry</topic><topic>Membranes - metabolism</topic><topic>Micelles</topic><topic>Models, Biological</topic><topic>Molecular biophysics</topic><topic>Molecular Sequence Data</topic><topic>neuropeptides</topic><topic>Neuropeptides - chemistry</topic><topic>Neuropeptides - metabolism</topic><topic>Sodium Dodecyl Sulfate</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>spectroscopy</topic><topic>U.V. radiation</topic><topic>Water - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Young, John K.</creatorcontrib><creatorcontrib>Graham, William H.</creatorcontrib><creatorcontrib>Beard, Debbie J.</creatorcontrib><creatorcontrib>Hicks, Rickey P.</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>Neurosciences Abstracts</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><jtitle>Biopolymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Young, John K.</au><au>Graham, William H.</au><au>Beard, Debbie J.</au><au>Hicks, Rickey P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The use of UV-visible spectroscopy for the determination of hydrophobic interactions between neuropeptides and membrane model systems</atitle><jtitle>Biopolymers</jtitle><addtitle>Biopolymers</addtitle><date>1992-08</date><risdate>1992</risdate><volume>32</volume><issue>8</issue><spage>1061</spage><epage>1064</epage><pages>1061-1064</pages><issn>0006-3525</issn><eissn>1097-0282</eissn><coden>BIPMAA</coden><abstract>Ultraviolet‐visible spectroscopy has been used as a rapid method to evaluate the hydrophobia interactions between a series of cationic and zwitterionic neuropeptides and dipeptides with the hydrophobia core of two membrane model systems; sodium dodecyl sulfate and lysophosphatidylcholine micelles. If a hydrophobia interaction occurs, a 1−nm bathochromic shift is observed in the uv‐visible spectrum of the aromatic side chains when going from aqueous solution to a micellar solution. The aromatic residues of substance P, bradykinin, and Des‐Arg9 bradykinin all exhibited the 1−nm bathochromic shift in the presence of sodium dodecyl sulfate while those of Met‐enkephalin did not. The opposite effects were observed in the presence of lysophosphatidylcholine micelles. © 1992 John Wiley & Sons, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>1420972</pmid><doi>10.1002/bip.360320815</doi><tpages>4</tpages></addata></record> |
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subjects | Amino Acid Sequence Biological and medical sciences Fundamental and applied biological sciences. Psychology hydrophobicity Interactions. Associations Intermolecular phenomena Lysophosphatidylcholines membranes Membranes - chemistry Membranes - metabolism Micelles Models, Biological Molecular biophysics Molecular Sequence Data neuropeptides Neuropeptides - chemistry Neuropeptides - metabolism Sodium Dodecyl Sulfate Spectrophotometry, Ultraviolet spectroscopy U.V. radiation Water - chemistry |
title | The use of UV-visible spectroscopy for the determination of hydrophobic interactions between neuropeptides and membrane model systems |
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