Trifluoroethanol induces the self-association of specific amphipathic peptides
We have examined the effect of trifluoroethanol (TFE) on the solution behaviour of three amphipathic peptides. One of the peptides, containing three heptad repeat units (Ac-YS-(AKEAAKE) 3GAR-NH 2), remained monomeric under conditions where TFE induced a two-state transition from a random coil to an...
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| Veröffentlicht in: | FEBS letters 1997-10, Vol.416 (3), p.265-268 |
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| creator | MacPhee, Cait E Perugini, Matthew A H. Sawyer, William Howlett, Geoffrey J |
| description | We have examined the effect of trifluoroethanol (TFE) on the solution behaviour of three amphipathic peptides. One of the peptides, containing three heptad repeat units (Ac-YS-(AKEAAKE)
3GAR-NH
2), remained monomeric under conditions where TFE induced a two-state transition from a random coil to an α-helix. In contrast, the TFE-induced α-helical formation of two peptides derived from human apolipoproteins C-II and E was accompanied by the formation of discrete dimers and trimers, respectively. The apolipoprotein C-II peptide further aggregated to form β-sheet at higher concentrations of TFE (50% v/v). The results suggest a class of peptides capable of discrete self-association in the presence of cosolvents which favour intramolecular hydrogen bonding. |
| doi_str_mv | 10.1016/S0014-5793(97)01224-6 |
| format | Article |
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3GAR-NH
2), remained monomeric under conditions where TFE induced a two-state transition from a random coil to an α-helix. In contrast, the TFE-induced α-helical formation of two peptides derived from human apolipoproteins C-II and E was accompanied by the formation of discrete dimers and trimers, respectively. The apolipoprotein C-II peptide further aggregated to form β-sheet at higher concentrations of TFE (50% v/v). The results suggest a class of peptides capable of discrete self-association in the presence of cosolvents which favour intramolecular hydrogen bonding.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(97)01224-6</identifier><identifier>PMID: 9373166</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>2,2,2-trifluoroethanol ; Amino Acid Sequence ; Analytical ultracentrifugation ; apo C-II ; apo E ; Apolipoprotein ; Apolipoprotein C-II ; apolipoprotein E ; Apolipoproteins C - chemistry ; Apolipoproteins C - drug effects ; Apolipoproteins E - chemistry ; Apolipoproteins E - drug effects ; Circular Dichroism ; Humans ; Hydrogen Bonding ; Lipid-peptide interaction ; mean residue ellipticity ; Molecular Sequence Data ; MRE ; Peptide Fragments - chemistry ; Peptide Fragments - drug effects ; Peptides - chemistry ; Peptides - drug effects ; Protein Structure, Secondary ; SDS ; sodium dodecyl sulphate ; TFA ; TFE ; trifluoroacetic acid ; Trifluoroethanol ; Trifluoroethanol - pharmacology ; Viscosity ; α-Helical peptide</subject><ispartof>FEBS letters, 1997-10, Vol.416 (3), p.265-268</ispartof><rights>1997 Federation of European Biochemical Societies</rights><rights>FEBS Letters 416 (1997) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4916-ad59dcbef68bb804c905f25e70ed82b6dc9c0d7b8c99cb37c410dfb32f43a4ef3</citedby><cites>FETCH-LOGICAL-c4916-ad59dcbef68bb804c905f25e70ed82b6dc9c0d7b8c99cb37c410dfb32f43a4ef3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2897%2901224-6$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(97)01224-6$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1416,1432,3548,27922,27923,45572,45573,45993,46407,46831</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9373166$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MacPhee, Cait E</creatorcontrib><creatorcontrib>Perugini, Matthew A</creatorcontrib><creatorcontrib>H. Sawyer, William</creatorcontrib><creatorcontrib>Howlett, Geoffrey J</creatorcontrib><title>Trifluoroethanol induces the self-association of specific amphipathic peptides</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>We have examined the effect of trifluoroethanol (TFE) on the solution behaviour of three amphipathic peptides. One of the peptides, containing three heptad repeat units (Ac-YS-(AKEAAKE)
3GAR-NH
2), remained monomeric under conditions where TFE induced a two-state transition from a random coil to an α-helix. In contrast, the TFE-induced α-helical formation of two peptides derived from human apolipoproteins C-II and E was accompanied by the formation of discrete dimers and trimers, respectively. The apolipoprotein C-II peptide further aggregated to form β-sheet at higher concentrations of TFE (50% v/v). The results suggest a class of peptides capable of discrete self-association in the presence of cosolvents which favour intramolecular hydrogen bonding.</description><subject>2,2,2-trifluoroethanol</subject><subject>Amino Acid Sequence</subject><subject>Analytical ultracentrifugation</subject><subject>apo C-II</subject><subject>apo E</subject><subject>Apolipoprotein</subject><subject>Apolipoprotein C-II</subject><subject>apolipoprotein E</subject><subject>Apolipoproteins C - chemistry</subject><subject>Apolipoproteins C - drug effects</subject><subject>Apolipoproteins E - chemistry</subject><subject>Apolipoproteins E - drug effects</subject><subject>Circular Dichroism</subject><subject>Humans</subject><subject>Hydrogen Bonding</subject><subject>Lipid-peptide interaction</subject><subject>mean residue ellipticity</subject><subject>Molecular Sequence Data</subject><subject>MRE</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - drug effects</subject><subject>Peptides - chemistry</subject><subject>Peptides - drug effects</subject><subject>Protein Structure, Secondary</subject><subject>SDS</subject><subject>sodium dodecyl sulphate</subject><subject>TFA</subject><subject>TFE</subject><subject>trifluoroacetic acid</subject><subject>Trifluoroethanol</subject><subject>Trifluoroethanol - pharmacology</subject><subject>Viscosity</subject><subject>α-Helical peptide</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMtu3CAUhlHVaDpN-wiRvKqahRswGMyqaka5SVGyyHSN8OGgofIYF-xEeft6Lso2XQHnvxz0EXLG6A9Gmbx4opSJslaaf9fqnLKqEqX8QJasUbzkQjYfyfLN8ol8zvkPnd8N0wuy0FxxJuWSPKxT8N0UU8RxY_vYFaF3E2Auxg0WGTtf2pwjBDuG2BfRF3lACD5AYbfDJgx23Mz3AYcxOMxfyIm3Xcavx_OU_L6-Wq9uy_vHm7vVr_sShGaytK7WDlr0smnbhgrQtPZVjYqia6pWOtBAnWob0BparkAw6nzLKy-4Fej5Kfl26B1S_DthHs02ZMCusz3GKRulBWt4Vc_G-mCEFHNO6M2QwtamV8Oo2XE0e45mB8loZfYcjZxzZ8cFU7tF95Y6gpv124P-Ejp8_b9Sc311We2VnaDVfryr-nmowhnYc8BkMgTsAV1ICKNxMbzz2X8bIJhK</recordid><startdate>19971027</startdate><enddate>19971027</enddate><creator>MacPhee, Cait E</creator><creator>Perugini, Matthew A</creator><creator>H. Sawyer, William</creator><creator>Howlett, Geoffrey J</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>19971027</creationdate><title>Trifluoroethanol induces the self-association of specific amphipathic peptides</title><author>MacPhee, Cait E ; Perugini, Matthew A ; H. Sawyer, William ; Howlett, Geoffrey J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4916-ad59dcbef68bb804c905f25e70ed82b6dc9c0d7b8c99cb37c410dfb32f43a4ef3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>2,2,2-trifluoroethanol</topic><topic>Amino Acid Sequence</topic><topic>Analytical ultracentrifugation</topic><topic>apo C-II</topic><topic>apo E</topic><topic>Apolipoprotein</topic><topic>Apolipoprotein C-II</topic><topic>apolipoprotein E</topic><topic>Apolipoproteins C - chemistry</topic><topic>Apolipoproteins C - drug effects</topic><topic>Apolipoproteins E - chemistry</topic><topic>Apolipoproteins E - drug effects</topic><topic>Circular Dichroism</topic><topic>Humans</topic><topic>Hydrogen Bonding</topic><topic>Lipid-peptide interaction</topic><topic>mean residue ellipticity</topic><topic>Molecular Sequence Data</topic><topic>MRE</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - drug effects</topic><topic>Peptides - chemistry</topic><topic>Peptides - drug effects</topic><topic>Protein Structure, Secondary</topic><topic>SDS</topic><topic>sodium dodecyl sulphate</topic><topic>TFA</topic><topic>TFE</topic><topic>trifluoroacetic acid</topic><topic>Trifluoroethanol</topic><topic>Trifluoroethanol - pharmacology</topic><topic>Viscosity</topic><topic>α-Helical peptide</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MacPhee, Cait E</creatorcontrib><creatorcontrib>Perugini, Matthew A</creatorcontrib><creatorcontrib>H. Sawyer, William</creatorcontrib><creatorcontrib>Howlett, Geoffrey J</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MacPhee, Cait E</au><au>Perugini, Matthew A</au><au>H. Sawyer, William</au><au>Howlett, Geoffrey J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Trifluoroethanol induces the self-association of specific amphipathic peptides</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1997-10-27</date><risdate>1997</risdate><volume>416</volume><issue>3</issue><spage>265</spage><epage>268</epage><pages>265-268</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>We have examined the effect of trifluoroethanol (TFE) on the solution behaviour of three amphipathic peptides. One of the peptides, containing three heptad repeat units (Ac-YS-(AKEAAKE)
3GAR-NH
2), remained monomeric under conditions where TFE induced a two-state transition from a random coil to an α-helix. In contrast, the TFE-induced α-helical formation of two peptides derived from human apolipoproteins C-II and E was accompanied by the formation of discrete dimers and trimers, respectively. The apolipoprotein C-II peptide further aggregated to form β-sheet at higher concentrations of TFE (50% v/v). The results suggest a class of peptides capable of discrete self-association in the presence of cosolvents which favour intramolecular hydrogen bonding.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9373166</pmid><doi>10.1016/S0014-5793(97)01224-6</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Wiley Online Library Free Content; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | 2,2,2-trifluoroethanol Amino Acid Sequence Analytical ultracentrifugation apo C-II apo E Apolipoprotein Apolipoprotein C-II apolipoprotein E Apolipoproteins C - chemistry Apolipoproteins C - drug effects Apolipoproteins E - chemistry Apolipoproteins E - drug effects Circular Dichroism Humans Hydrogen Bonding Lipid-peptide interaction mean residue ellipticity Molecular Sequence Data MRE Peptide Fragments - chemistry Peptide Fragments - drug effects Peptides - chemistry Peptides - drug effects Protein Structure, Secondary SDS sodium dodecyl sulphate TFA TFE trifluoroacetic acid Trifluoroethanol Trifluoroethanol - pharmacology Viscosity α-Helical peptide |
| title | Trifluoroethanol induces the self-association of specific amphipathic peptides |
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