The relationship between peptide structure and antibacterial activity
Cationic antimicrobial peptides are a class of small, positively charged peptides known for their broad-spectrum antimicrobial activity. These peptides have also been shown to possess anti-viral and anti-cancer activity and, most recently, the ability to modulate the innate immune response. To date,...
Gespeichert in:
| Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2003-11, Vol.24 (11), p.1681-1691 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1691 |
|---|---|
| container_issue | 11 |
| container_start_page | 1681 |
| container_title | Peptides (New York, N.Y. : 1980) |
| container_volume | 24 |
| creator | Powers, Jon-Paul S Hancock, Robert E.W |
| description | Cationic antimicrobial peptides are a class of small, positively charged peptides known for their broad-spectrum antimicrobial activity. These peptides have also been shown to possess anti-viral and anti-cancer activity and, most recently, the ability to modulate the innate immune response. To date, a large number of antimicrobial peptides have been chemically characterized, however, few high-resolution structures are available. Structure–activity studies of these peptides reveal two main requirements for antimicrobial activity, (1) a cationic charge and (2) an induced amphipathic conformation. In addition to peptide conformation, the role of membrane lipid composition, specifically non-bilayer lipids, on peptide activity will also be discussed. |
| doi_str_mv | 10.1016/j.peptides.2003.08.023 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71543421</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0196978103003425</els_id><sourcerecordid>71543421</sourcerecordid><originalsourceid>FETCH-LOGICAL-c461t-1d30a13ea3f301ffabf679b61309cba81e564af5aa594b43a261372a7ab3ff0c3</originalsourceid><addsrcrecordid>eNqFkE1LxDAQhoMoun78BenJW2umadPmpohfIHjRc5imE8zSbWuSKv57I7vi0cMwA_PMvPAwdg68AA7ycl3MNEfXUyhKzkXB24KXYo-toG1EXoNU-2zFQclcNS0cseMQ1pzzqlLtITuCOq1AqRW7fXmjzNOA0U1jeHNz1lH8JBqz3f8sRL-YuHjKcOxTRdehieQdDlka3IeLX6fswOIQ6GzXT9jr3e3LzUP-9Hz_eHP9lJtKQsyhFxxBEAorOFiLnZWN6iQIrkyHLVAtK7Q1Yq2qrhJYplVTYoOdsJYbccIutn9nP70vFKLeuGBoGHCkaQm6gboSVQn_gqDKupRSJlBuQeOnEDxZPXu3Qf-lgesf03qtf03rH9OatzqZTofnu4Sl21D_d7ZTm4CrLUBJyIcjr4NxNBrqnScTdT-5_zK-AdIvk_8</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19252666</pqid></control><display><type>article</type><title>The relationship between peptide structure and antibacterial activity</title><source>Elsevier ScienceDirect Journals Complete - AutoHoldings</source><source>MEDLINE</source><creator>Powers, Jon-Paul S ; Hancock, Robert E.W</creator><creatorcontrib>Powers, Jon-Paul S ; Hancock, Robert E.W</creatorcontrib><description>Cationic antimicrobial peptides are a class of small, positively charged peptides known for their broad-spectrum antimicrobial activity. These peptides have also been shown to possess anti-viral and anti-cancer activity and, most recently, the ability to modulate the innate immune response. To date, a large number of antimicrobial peptides have been chemically characterized, however, few high-resolution structures are available. Structure–activity studies of these peptides reveal two main requirements for antimicrobial activity, (1) a cationic charge and (2) an induced amphipathic conformation. In addition to peptide conformation, the role of membrane lipid composition, specifically non-bilayer lipids, on peptide activity will also be discussed.</description><identifier>ISSN: 0196-9781</identifier><identifier>EISSN: 1873-5169</identifier><identifier>DOI: 10.1016/j.peptides.2003.08.023</identifier><identifier>PMID: 15019199</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Antimicrobial cationic peptide ; Antimicrobial Cationic Peptides - chemistry ; Antimicrobial Cationic Peptides - metabolism ; Antimicrobial Cationic Peptides - pharmacology ; Cell Membrane - metabolism ; Membrane Lipids - chemistry ; Membrane Lipids - metabolism ; Polyphemusin ; Protein Conformation ; Structure ; Structure-Activity Relationship</subject><ispartof>Peptides (New York, N.Y. : 1980), 2003-11, Vol.24 (11), p.1681-1691</ispartof><rights>2003 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c461t-1d30a13ea3f301ffabf679b61309cba81e564af5aa594b43a261372a7ab3ff0c3</citedby><cites>FETCH-LOGICAL-c461t-1d30a13ea3f301ffabf679b61309cba81e564af5aa594b43a261372a7ab3ff0c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.peptides.2003.08.023$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27907,27908,45978</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15019199$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Powers, Jon-Paul S</creatorcontrib><creatorcontrib>Hancock, Robert E.W</creatorcontrib><title>The relationship between peptide structure and antibacterial activity</title><title>Peptides (New York, N.Y. : 1980)</title><addtitle>Peptides</addtitle><description>Cationic antimicrobial peptides are a class of small, positively charged peptides known for their broad-spectrum antimicrobial activity. These peptides have also been shown to possess anti-viral and anti-cancer activity and, most recently, the ability to modulate the innate immune response. To date, a large number of antimicrobial peptides have been chemically characterized, however, few high-resolution structures are available. Structure–activity studies of these peptides reveal two main requirements for antimicrobial activity, (1) a cationic charge and (2) an induced amphipathic conformation. In addition to peptide conformation, the role of membrane lipid composition, specifically non-bilayer lipids, on peptide activity will also be discussed.</description><subject>Animals</subject><subject>Antimicrobial cationic peptide</subject><subject>Antimicrobial Cationic Peptides - chemistry</subject><subject>Antimicrobial Cationic Peptides - metabolism</subject><subject>Antimicrobial Cationic Peptides - pharmacology</subject><subject>Cell Membrane - metabolism</subject><subject>Membrane Lipids - chemistry</subject><subject>Membrane Lipids - metabolism</subject><subject>Polyphemusin</subject><subject>Protein Conformation</subject><subject>Structure</subject><subject>Structure-Activity Relationship</subject><issn>0196-9781</issn><issn>1873-5169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAQhoMoun78BenJW2umadPmpohfIHjRc5imE8zSbWuSKv57I7vi0cMwA_PMvPAwdg68AA7ycl3MNEfXUyhKzkXB24KXYo-toG1EXoNU-2zFQclcNS0cseMQ1pzzqlLtITuCOq1AqRW7fXmjzNOA0U1jeHNz1lH8JBqz3f8sRL-YuHjKcOxTRdehieQdDlka3IeLX6fswOIQ6GzXT9jr3e3LzUP-9Hz_eHP9lJtKQsyhFxxBEAorOFiLnZWN6iQIrkyHLVAtK7Q1Yq2qrhJYplVTYoOdsJYbccIutn9nP70vFKLeuGBoGHCkaQm6gboSVQn_gqDKupRSJlBuQeOnEDxZPXu3Qf-lgesf03qtf03rH9OatzqZTofnu4Sl21D_d7ZTm4CrLUBJyIcjr4NxNBrqnScTdT-5_zK-AdIvk_8</recordid><startdate>20031101</startdate><enddate>20031101</enddate><creator>Powers, Jon-Paul S</creator><creator>Hancock, Robert E.W</creator><general>Elsevier Inc</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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20031101</creationdate><title>The relationship between peptide structure and antibacterial activity</title><author>Powers, Jon-Paul S ; Hancock, Robert E.W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c461t-1d30a13ea3f301ffabf679b61309cba81e564af5aa594b43a261372a7ab3ff0c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Antimicrobial cationic peptide</topic><topic>Antimicrobial Cationic Peptides - chemistry</topic><topic>Antimicrobial Cationic Peptides - metabolism</topic><topic>Antimicrobial Cationic Peptides - pharmacology</topic><topic>Cell Membrane - metabolism</topic><topic>Membrane Lipids - chemistry</topic><topic>Membrane Lipids - metabolism</topic><topic>Polyphemusin</topic><topic>Protein Conformation</topic><topic>Structure</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Powers, Jon-Paul S</creatorcontrib><creatorcontrib>Hancock, Robert E.W</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Peptides (New York, N.Y. : 1980)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Powers, Jon-Paul S</au><au>Hancock, Robert E.W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The relationship between peptide structure and antibacterial activity</atitle><jtitle>Peptides (New York, N.Y. : 1980)</jtitle><addtitle>Peptides</addtitle><date>2003-11-01</date><risdate>2003</risdate><volume>24</volume><issue>11</issue><spage>1681</spage><epage>1691</epage><pages>1681-1691</pages><issn>0196-9781</issn><eissn>1873-5169</eissn><abstract>Cationic antimicrobial peptides are a class of small, positively charged peptides known for their broad-spectrum antimicrobial activity. These peptides have also been shown to possess anti-viral and anti-cancer activity and, most recently, the ability to modulate the innate immune response. To date, a large number of antimicrobial peptides have been chemically characterized, however, few high-resolution structures are available. Structure–activity studies of these peptides reveal two main requirements for antimicrobial activity, (1) a cationic charge and (2) an induced amphipathic conformation. In addition to peptide conformation, the role of membrane lipid composition, specifically non-bilayer lipids, on peptide activity will also be discussed.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15019199</pmid><doi>10.1016/j.peptides.2003.08.023</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0196-9781 |
| ispartof | Peptides (New York, N.Y. : 1980), 2003-11, Vol.24 (11), p.1681-1691 |
| issn | 0196-9781 1873-5169 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71543421 |
| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE |
| subjects | Animals Antimicrobial cationic peptide Antimicrobial Cationic Peptides - chemistry Antimicrobial Cationic Peptides - metabolism Antimicrobial Cationic Peptides - pharmacology Cell Membrane - metabolism Membrane Lipids - chemistry Membrane Lipids - metabolism Polyphemusin Protein Conformation Structure Structure-Activity Relationship |
| title | The relationship between peptide structure and antibacterial activity |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-16T06%3A19%3A00IST&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=The%20relationship%20between%20peptide%20structure%20and%20antibacterial%20activity&rft.jtitle=Peptides%20(New%20York,%20N.Y.%20:%201980)&rft.au=Powers,%20Jon-Paul%20S&rft.date=2003-11-01&rft.volume=24&rft.issue=11&rft.spage=1681&rft.epage=1691&rft.pages=1681-1691&rft.issn=0196-9781&rft.eissn=1873-5169&rft_id=info:doi/10.1016/j.peptides.2003.08.023&rft_dat=%3Cproquest_cross%3E71543421%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=19252666&rft_id=info:pmid/15019199&rft_els_id=S0196978103003425&rfr_iscdi=true |