Intrinsic flexibility and structural adaptability of Plasticins membrane-damaging peptides as a strategy for functional versatility
The Plasticins are a family of antimicrobial, 23-29-residue Gly-Leu-rich ortholog peptides from the frog skin that have very similar amino acid sequences, hydrophobicities, and amphipathicities but differ markedly in their conformational plasticity and spectrum of activity. The intrinsic flexibility...
Gespeichert in:
| Veröffentlicht in: | European biophysics journal 2007-11, Vol.36 (8), p.901-909 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 909 |
|---|---|
| container_issue | 8 |
| container_start_page | 901 |
| container_title | European biophysics journal |
| container_volume | 36 |
| creator | El Amri, C Bruston, F Joanne, P Lacombe, C Nicolas, P |
| description | The Plasticins are a family of antimicrobial, 23-29-residue Gly-Leu-rich ortholog peptides from the frog skin that have very similar amino acid sequences, hydrophobicities, and amphipathicities but differ markedly in their conformational plasticity and spectrum of activity. The intrinsic flexibility and structural malleability of Plasticins modulate their ability to bind to and disrupt the bilayer membranes of prokaryotic and eukaryotic cells, and/or to reach intracellular targets, therefore, triggering functional versatility. The discussion is opened herein on several examples of other membrane-active peptides, like viral fusion peptides, cell-penetrating peptides, that are able to display antimicrobial activity. Hence, Plasticins could be regarded as models of multipotent membrane-active peptides guided by structural plasticity. |
| doi_str_mv | 10.1007/s00249-007-0199-2 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_754564974</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>754564974</sourcerecordid><originalsourceid>FETCH-LOGICAL-c358t-d9ff86eb3b8b7b6884939135cdaaf2b807ba5038ab909f1ecf2bce1f6ba9059d3</originalsourceid><addsrcrecordid>eNp9kU1rHSEUhqWkNDdpf0A3RbJoVrbq6KjLEtIkEGgX7Xo4OnoxzFfVKbnr_vE6vRcKXRRED_qchyMvQm8Z_cAoVR8zpVwYUktCmTGEv0A7JhpOGGXqDO3qLomSip2ji5yfKBWSMf0KnTPVci652KFfD1NJccrR4TD452jjEMsBw9TjXNLqyppgwNDDUuD0Ngf8dYBcoqt9ePSjTTB50sMI-zjt8eKXEnufMdS1WaD4_QGHOeGwTq7EearKnz5lKH-Mr9HLAEP2b07nJfr--fbbzT15_HL3cPPpkbhG6kJ6E4JuvW2stsq2WgvTGNZI1wMEbjVVFiRtNFhDTWDe1UvnWWgtGCpN31yi66N3SfOP1efSjTE7Pwx1_HnNnZJCtsIoUcn3_yVbLaSUdAOv_gGf5jXV_1WGK9Gy6qsQO0IuzTknH7olxRHSoWO024LsjkF2W7kF2fHa8-4kXu3o-78dp-Sa37aBnH4</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>627461649</pqid></control><display><type>article</type><title>Intrinsic flexibility and structural adaptability of Plasticins membrane-damaging peptides as a strategy for functional versatility</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><creator>El Amri, C ; Bruston, F ; Joanne, P ; Lacombe, C ; Nicolas, P</creator><creatorcontrib>El Amri, C ; Bruston, F ; Joanne, P ; Lacombe, C ; Nicolas, P</creatorcontrib><description>The Plasticins are a family of antimicrobial, 23-29-residue Gly-Leu-rich ortholog peptides from the frog skin that have very similar amino acid sequences, hydrophobicities, and amphipathicities but differ markedly in their conformational plasticity and spectrum of activity. The intrinsic flexibility and structural malleability of Plasticins modulate their ability to bind to and disrupt the bilayer membranes of prokaryotic and eukaryotic cells, and/or to reach intracellular targets, therefore, triggering functional versatility. The discussion is opened herein on several examples of other membrane-active peptides, like viral fusion peptides, cell-penetrating peptides, that are able to display antimicrobial activity. Hence, Plasticins could be regarded as models of multipotent membrane-active peptides guided by structural plasticity.</description><identifier>ISSN: 0175-7571</identifier><identifier>EISSN: 1432-1017</identifier><identifier>DOI: 10.1007/s00249-007-0199-2</identifier><identifier>PMID: 17622524</identifier><language>eng</language><publisher>Germany: Springer Nature B.V</publisher><subject>Adaptability ; Amino Acid Sequence ; Amino acids ; Animals ; Anti-Bacterial Agents - chemistry ; Antimicrobial agents ; Anura ; Bacteria ; Eye Proteins - chemistry ; Humans ; Membranes ; Membranes - chemistry ; Membranes - drug effects ; Microbiology ; Models, Molecular ; Molecular Sequence Data ; Nerve Tissue Proteins - chemistry ; Peptides ; Plasticity ; Protein Conformation ; Proteins</subject><ispartof>European biophysics journal, 2007-11, Vol.36 (8), p.901-909</ispartof><rights>EBSA 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c358t-d9ff86eb3b8b7b6884939135cdaaf2b807ba5038ab909f1ecf2bce1f6ba9059d3</citedby><cites>FETCH-LOGICAL-c358t-d9ff86eb3b8b7b6884939135cdaaf2b807ba5038ab909f1ecf2bce1f6ba9059d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17622524$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>El Amri, C</creatorcontrib><creatorcontrib>Bruston, F</creatorcontrib><creatorcontrib>Joanne, P</creatorcontrib><creatorcontrib>Lacombe, C</creatorcontrib><creatorcontrib>Nicolas, P</creatorcontrib><title>Intrinsic flexibility and structural adaptability of Plasticins membrane-damaging peptides as a strategy for functional versatility</title><title>European biophysics journal</title><addtitle>Eur Biophys J</addtitle><description>The Plasticins are a family of antimicrobial, 23-29-residue Gly-Leu-rich ortholog peptides from the frog skin that have very similar amino acid sequences, hydrophobicities, and amphipathicities but differ markedly in their conformational plasticity and spectrum of activity. The intrinsic flexibility and structural malleability of Plasticins modulate their ability to bind to and disrupt the bilayer membranes of prokaryotic and eukaryotic cells, and/or to reach intracellular targets, therefore, triggering functional versatility. The discussion is opened herein on several examples of other membrane-active peptides, like viral fusion peptides, cell-penetrating peptides, that are able to display antimicrobial activity. Hence, Plasticins could be regarded as models of multipotent membrane-active peptides guided by structural plasticity.</description><subject>Adaptability</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Antimicrobial agents</subject><subject>Anura</subject><subject>Bacteria</subject><subject>Eye Proteins - chemistry</subject><subject>Humans</subject><subject>Membranes</subject><subject>Membranes - chemistry</subject><subject>Membranes - drug effects</subject><subject>Microbiology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Peptides</subject><subject>Plasticity</subject><subject>Protein Conformation</subject><subject>Proteins</subject><issn>0175-7571</issn><issn>1432-1017</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kU1rHSEUhqWkNDdpf0A3RbJoVrbq6KjLEtIkEGgX7Xo4OnoxzFfVKbnr_vE6vRcKXRRED_qchyMvQm8Z_cAoVR8zpVwYUktCmTGEv0A7JhpOGGXqDO3qLomSip2ji5yfKBWSMf0KnTPVci652KFfD1NJccrR4TD452jjEMsBw9TjXNLqyppgwNDDUuD0Ngf8dYBcoqt9ePSjTTB50sMI-zjt8eKXEnufMdS1WaD4_QGHOeGwTq7EearKnz5lKH-Mr9HLAEP2b07nJfr--fbbzT15_HL3cPPpkbhG6kJ6E4JuvW2stsq2WgvTGNZI1wMEbjVVFiRtNFhDTWDe1UvnWWgtGCpN31yi66N3SfOP1efSjTE7Pwx1_HnNnZJCtsIoUcn3_yVbLaSUdAOv_gGf5jXV_1WGK9Gy6qsQO0IuzTknH7olxRHSoWO024LsjkF2W7kF2fHa8-4kXu3o-78dp-Sa37aBnH4</recordid><startdate>20071101</startdate><enddate>20071101</enddate><creator>El Amri, C</creator><creator>Bruston, F</creator><creator>Joanne, P</creator><creator>Lacombe, C</creator><creator>Nicolas, P</creator><general>Springer Nature B.V</general><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>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20071101</creationdate><title>Intrinsic flexibility and structural adaptability of Plasticins membrane-damaging peptides as a strategy for functional versatility</title><author>El Amri, C ; Bruston, F ; Joanne, P ; Lacombe, C ; Nicolas, P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c358t-d9ff86eb3b8b7b6884939135cdaaf2b807ba5038ab909f1ecf2bce1f6ba9059d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adaptability</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Anti-Bacterial Agents - chemistry</topic><topic>Antimicrobial agents</topic><topic>Anura</topic><topic>Bacteria</topic><topic>Eye Proteins - chemistry</topic><topic>Humans</topic><topic>Membranes</topic><topic>Membranes - chemistry</topic><topic>Membranes - drug effects</topic><topic>Microbiology</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Peptides</topic><topic>Plasticity</topic><topic>Protein Conformation</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>El Amri, C</creatorcontrib><creatorcontrib>Bruston, F</creatorcontrib><creatorcontrib>Joanne, P</creatorcontrib><creatorcontrib>Lacombe, C</creatorcontrib><creatorcontrib>Nicolas, P</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>European biophysics journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>El Amri, C</au><au>Bruston, F</au><au>Joanne, P</au><au>Lacombe, C</au><au>Nicolas, P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Intrinsic flexibility and structural adaptability of Plasticins membrane-damaging peptides as a strategy for functional versatility</atitle><jtitle>European biophysics journal</jtitle><addtitle>Eur Biophys J</addtitle><date>2007-11-01</date><risdate>2007</risdate><volume>36</volume><issue>8</issue><spage>901</spage><epage>909</epage><pages>901-909</pages><issn>0175-7571</issn><eissn>1432-1017</eissn><abstract>The Plasticins are a family of antimicrobial, 23-29-residue Gly-Leu-rich ortholog peptides from the frog skin that have very similar amino acid sequences, hydrophobicities, and amphipathicities but differ markedly in their conformational plasticity and spectrum of activity. The intrinsic flexibility and structural malleability of Plasticins modulate their ability to bind to and disrupt the bilayer membranes of prokaryotic and eukaryotic cells, and/or to reach intracellular targets, therefore, triggering functional versatility. The discussion is opened herein on several examples of other membrane-active peptides, like viral fusion peptides, cell-penetrating peptides, that are able to display antimicrobial activity. Hence, Plasticins could be regarded as models of multipotent membrane-active peptides guided by structural plasticity.</abstract><cop>Germany</cop><pub>Springer Nature B.V</pub><pmid>17622524</pmid><doi>10.1007/s00249-007-0199-2</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0175-7571 |
| ispartof | European biophysics journal, 2007-11, Vol.36 (8), p.901-909 |
| issn | 0175-7571 1432-1017 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_754564974 |
| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Adaptability Amino Acid Sequence Amino acids Animals Anti-Bacterial Agents - chemistry Antimicrobial agents Anura Bacteria Eye Proteins - chemistry Humans Membranes Membranes - chemistry Membranes - drug effects Microbiology Models, Molecular Molecular Sequence Data Nerve Tissue Proteins - chemistry Peptides Plasticity Protein Conformation Proteins |
| title | Intrinsic flexibility and structural adaptability of Plasticins membrane-damaging peptides as a strategy for functional versatility |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-21T13%3A52%3A02IST&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=Intrinsic%20flexibility%20and%20structural%20adaptability%20of%20Plasticins%20membrane-damaging%20peptides%20as%20a%20strategy%20for%20functional%20versatility&rft.jtitle=European%20biophysics%20journal&rft.au=El%20Amri,%20C&rft.date=2007-11-01&rft.volume=36&rft.issue=8&rft.spage=901&rft.epage=909&rft.pages=901-909&rft.issn=0175-7571&rft.eissn=1432-1017&rft_id=info:doi/10.1007/s00249-007-0199-2&rft_dat=%3Cproquest_cross%3E754564974%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=627461649&rft_id=info:pmid/17622524&rfr_iscdi=true |