Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy
The conformational properties of the magainin family of antimicrobial peptides in aqueous solution and in model membranes have been probed by Fourier transform infrared spectroscopy. The magainins were found to be structureless in aqueous solution at neutral pD, confirming other studies by Raman and...
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| Veröffentlicht in: | Biochemistry (Easton) 1992-08, Vol.31 (32), p.7289-7293 |
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| creator | Jackson, Michael Mantsch, Henry H Spencer, John H |
| description | The conformational properties of the magainin family of antimicrobial peptides in aqueous solution and in model membranes have been probed by Fourier transform infrared spectroscopy. The magainins were found to be structureless in aqueous solution at neutral pD, confirming other studies by Raman and circular dichroism spectroscopy. Increasing the pD to 10 induced the formation of predominantly alpha-helical secondary structures, with some beta-sheet. In the presence of negatively charged liposomes (dimyristoylphosphatidylglycerol), the peptides folded into alpha-helical secondary structures with some beta-sheet structure evident. On the other hand, in the presence of zwitterionic phospholipids (dimyristoylphosphatidylcholine), the spectra were identical to those in aqueous solution. For some magainins, the interaction with charged liposomes was modulated by the presence of cholesterol; cholesterol was found to promote the formation of beta-sheet structures, as evidenced by the appearance of amide I bands at 1614 and 1637 cm-1. Differences in structure were observed between the amidated and nonamidated forms of some peptides. From the data, a mechanism of antimicrobial action of the magainin family of peptides is proposed. |
| doi_str_mv | 10.1021/bi00147a012 |
| format | Article |
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The magainins were found to be structureless in aqueous solution at neutral pD, confirming other studies by Raman and circular dichroism spectroscopy. Increasing the pD to 10 induced the formation of predominantly alpha-helical secondary structures, with some beta-sheet. In the presence of negatively charged liposomes (dimyristoylphosphatidylglycerol), the peptides folded into alpha-helical secondary structures with some beta-sheet structure evident. On the other hand, in the presence of zwitterionic phospholipids (dimyristoylphosphatidylcholine), the spectra were identical to those in aqueous solution. For some magainins, the interaction with charged liposomes was modulated by the presence of cholesterol; cholesterol was found to promote the formation of beta-sheet structures, as evidenced by the appearance of amide I bands at 1614 and 1637 cm-1. Differences in structure were observed between the amidated and nonamidated forms of some peptides. From the data, a mechanism of antimicrobial action of the magainin family of peptides is proposed.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00147a012</identifier><identifier>PMID: 1510920</identifier><language>eng</language><publisher>WASHINGTON: American Chemical Society</publisher><subject>Amino Acid Sequence ; Aminoacids, peptides. Hormones. Neuropeptides ; Analytical, structural and metabolic biochemistry ; Animals ; Antimicrobial Cationic Peptides ; Biochemistry & Molecular Biology ; Biological and medical sciences ; Dimyristoylphosphatidylcholine ; Fourier Analysis ; Fundamental and applied biological sciences. Psychology ; I.R. spectroscopy ; Life Sciences & Biomedicine ; Liposomes ; magainin 2 ; Magainins ; Molecular Sequence Data ; Oligopeptides - chemistry ; Peptide Fragments - chemistry ; Peptides - chemical synthesis ; Peptides - chemistry ; Phosphatidylglycerols ; Protein Conformation ; Proteins ; Science & Technology ; Sequence Homology, Nucleic Acid ; skin ; solutions ; Spectrophotometry, Infrared ; structure ; Xenopus ; Xenopus laevis ; Xenopus Proteins</subject><ispartof>Biochemistry (Easton), 1992-08, Vol.31 (32), p.7289-7293</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>92</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wosA1992JJ57800012</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-a480t-c0e355c090fb69d39f24b856e248585ca5b5e8c59c30257bbe45636ab7ca069c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00147a012$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00147a012$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>315,781,785,2766,27080,27928,27929,56742,56792</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5514460$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1510920$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jackson, Michael</creatorcontrib><creatorcontrib>Mantsch, Henry H</creatorcontrib><creatorcontrib>Spencer, John H</creatorcontrib><title>Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy</title><title>Biochemistry (Easton)</title><addtitle>BIOCHEMISTRY-US</addtitle><addtitle>Biochemistry</addtitle><description>The conformational properties of the magainin family of antimicrobial peptides in aqueous solution and in model membranes have been probed by Fourier transform infrared spectroscopy. The magainins were found to be structureless in aqueous solution at neutral pD, confirming other studies by Raman and circular dichroism spectroscopy. Increasing the pD to 10 induced the formation of predominantly alpha-helical secondary structures, with some beta-sheet. In the presence of negatively charged liposomes (dimyristoylphosphatidylglycerol), the peptides folded into alpha-helical secondary structures with some beta-sheet structure evident. On the other hand, in the presence of zwitterionic phospholipids (dimyristoylphosphatidylcholine), the spectra were identical to those in aqueous solution. For some magainins, the interaction with charged liposomes was modulated by the presence of cholesterol; cholesterol was found to promote the formation of beta-sheet structures, as evidenced by the appearance of amide I bands at 1614 and 1637 cm-1. Differences in structure were observed between the amidated and nonamidated forms of some peptides. From the data, a mechanism of antimicrobial action of the magainin family of peptides is proposed.</description><subject>Amino Acid Sequence</subject><subject>Aminoacids, peptides. Hormones. Neuropeptides</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Antimicrobial Cationic Peptides</subject><subject>Biochemistry & Molecular Biology</subject><subject>Biological and medical sciences</subject><subject>Dimyristoylphosphatidylcholine</subject><subject>Fourier Analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>I.R. spectroscopy</subject><subject>Life Sciences & Biomedicine</subject><subject>Liposomes</subject><subject>magainin 2</subject><subject>Magainins</subject><subject>Molecular Sequence Data</subject><subject>Oligopeptides - chemistry</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - chemistry</subject><subject>Phosphatidylglycerols</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Science & Technology</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>skin</subject><subject>solutions</subject><subject>Spectrophotometry, Infrared</subject><subject>structure</subject><subject>Xenopus</subject><subject>Xenopus laevis</subject><subject>Xenopus Proteins</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EZCTM</sourceid><sourceid>EIF</sourceid><recordid>eNqNkk9vFSEUxSdGU2t15dqEhdGFGQUGmGHZTKy1qdGkdeOGAO-Ooc7AFBj1fQq_srw_eXVhoisC93fu5XCoqqcEvyaYkjfGYUxYqzGh96pjwimumZT8fnWMMRY1lQI_rB6ldFO2DLfsqDoinGBJ8XH1qw9-CHHS2QWPwoAm_VU773xNkfYrFGHUGVZohjm7FSTkPNK3C4QloRTGZSvbgBNMJmoPCPx3F4OfwOeE5hhMUZs1OgtLdBBRLlDaTCydhqhjqaYZbI4h2TCvH1cPBj0meLJfT6rPZ2-v-_P68uO79_3pZa1Zh3NtMTScWyzxYIRcNXKgzHRcAGUd77jV3HDoLJe2wZS3xgDjohHatFZjUU5Pqhe7vuWGxU7KanLJwjgWC8WbahsimOjEP0EihOzoFny1A22xkiIMao5u0nGtCFabnNQfORX62b7tYiZY3bG7YEr9-b6uk9VjeSlvXTpgnBPGBL4b-gNMGJJ14C0cqFMiJb244G1Xkt8O7f6f7l3efoo-LD4Xab2TupTh50Gj4zcl2qbl6vrTlerOO_rlqhfqQ-Ff7nhtk7op2fuS5l9f4jd6bNmS</recordid><startdate>199208</startdate><enddate>199208</enddate><creator>Jackson, Michael</creator><creator>Mantsch, Henry H</creator><creator>Spencer, John H</creator><general>American Chemical Society</general><general>Amer Chemical Soc</general><scope>BSCLL</scope><scope>BLEPL</scope><scope>DTL</scope><scope>EZCTM</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></search><sort><creationdate>199208</creationdate><title>Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy</title><author>Jackson, Michael ; Mantsch, Henry H ; Spencer, John H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a480t-c0e355c090fb69d39f24b856e248585ca5b5e8c59c30257bbe45636ab7ca069c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Aminoacids, peptides. Hormones. Neuropeptides</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Antimicrobial Cationic Peptides</topic><topic>Biochemistry & Molecular Biology</topic><topic>Biological and medical sciences</topic><topic>Dimyristoylphosphatidylcholine</topic><topic>Fourier Analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>I.R. spectroscopy</topic><topic>Life Sciences & Biomedicine</topic><topic>Liposomes</topic><topic>magainin 2</topic><topic>Magainins</topic><topic>Molecular Sequence Data</topic><topic>Oligopeptides - chemistry</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - chemistry</topic><topic>Phosphatidylglycerols</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Science & Technology</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>skin</topic><topic>solutions</topic><topic>Spectrophotometry, Infrared</topic><topic>structure</topic><topic>Xenopus</topic><topic>Xenopus laevis</topic><topic>Xenopus Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jackson, Michael</creatorcontrib><creatorcontrib>Mantsch, Henry H</creatorcontrib><creatorcontrib>Spencer, John H</creatorcontrib><collection>Istex</collection><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - Science Citation Index Expanded - 1992</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><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jackson, Michael</au><au>Mantsch, Henry H</au><au>Spencer, John H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy</atitle><jtitle>Biochemistry (Easton)</jtitle><stitle>BIOCHEMISTRY-US</stitle><addtitle>Biochemistry</addtitle><date>1992-08</date><risdate>1992</risdate><volume>31</volume><issue>32</issue><spage>7289</spage><epage>7293</epage><pages>7289-7293</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The conformational properties of the magainin family of antimicrobial peptides in aqueous solution and in model membranes have been probed by Fourier transform infrared spectroscopy. The magainins were found to be structureless in aqueous solution at neutral pD, confirming other studies by Raman and circular dichroism spectroscopy. Increasing the pD to 10 induced the formation of predominantly alpha-helical secondary structures, with some beta-sheet. In the presence of negatively charged liposomes (dimyristoylphosphatidylglycerol), the peptides folded into alpha-helical secondary structures with some beta-sheet structure evident. On the other hand, in the presence of zwitterionic phospholipids (dimyristoylphosphatidylcholine), the spectra were identical to those in aqueous solution. For some magainins, the interaction with charged liposomes was modulated by the presence of cholesterol; cholesterol was found to promote the formation of beta-sheet structures, as evidenced by the appearance of amide I bands at 1614 and 1637 cm-1. Differences in structure were observed between the amidated and nonamidated forms of some peptides. From the data, a mechanism of antimicrobial action of the magainin family of peptides is proposed.</abstract><cop>WASHINGTON</cop><pub>American Chemical Society</pub><pmid>1510920</pmid><doi>10.1021/bi00147a012</doi><tpages>5</tpages></addata></record> |
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| subjects | Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Animals Antimicrobial Cationic Peptides Biochemistry & Molecular Biology Biological and medical sciences Dimyristoylphosphatidylcholine Fourier Analysis Fundamental and applied biological sciences. Psychology I.R. spectroscopy Life Sciences & Biomedicine Liposomes magainin 2 Magainins Molecular Sequence Data Oligopeptides - chemistry Peptide Fragments - chemistry Peptides - chemical synthesis Peptides - chemistry Phosphatidylglycerols Protein Conformation Proteins Science & Technology Sequence Homology, Nucleic Acid skin solutions Spectrophotometry, Infrared structure Xenopus Xenopus laevis Xenopus Proteins |
| title | Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy |
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