Semisynthetic Approaches to Laspartomycin Analogues
Laspartomycin C (1), a lipopeptide antibiotic related to amphomycin, consists of a cyclic peptide core and an aspartic acid unit external to the core and linking this to a C15-2,3-unsaturated fatty acid. This was reported initially to be active against Staphylococcus aureus, and more recent studies...
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| Veröffentlicht in: | Journal of natural products (Washington, D.C.) D.C.), 2007-03, Vol.70 (3), p.447-450 |
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| container_title | Journal of natural products (Washington, D.C.) |
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| creator | Curran, William V Leese, Richard A Jarolmen, Howard Borders, Donald B Dugourd, Dominique Chen, Yuchen Cameron, Dale R |
| description | Laspartomycin C (1), a lipopeptide antibiotic related to amphomycin, consists of a cyclic peptide core and an aspartic acid unit external to the core and linking this to a C15-2,3-unsaturated fatty acid. This was reported initially to be active against Staphylococcus aureus, and more recent studies have shown that it is active against VRE, VISA, and MRSA isolates. The enzymatic cleavage of the fatty acid tail was accomplished with a deacylase produced by Actinoplanes utahensis and resulted in two peptides, designated Peptide 1 and Peptide 2. Semisynthetic derivatives of both peptides have been made, and the principal requirement for biological activity appears to be the presence of an acylaspartic acid. |
| doi_str_mv | 10.1021/np068062b |
| format | Article |
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This was reported initially to be active against Staphylococcus aureus, and more recent studies have shown that it is active against VRE, VISA, and MRSA isolates. The enzymatic cleavage of the fatty acid tail was accomplished with a deacylase produced by Actinoplanes utahensis and resulted in two peptides, designated Peptide 1 and Peptide 2. Semisynthetic derivatives of both peptides have been made, and the principal requirement for biological activity appears to be the presence of an acylaspartic acid.</description><identifier>ISSN: 0163-3864</identifier><identifier>EISSN: 1520-6025</identifier><identifier>DOI: 10.1021/np068062b</identifier><identifier>PMID: 17323996</identifier><identifier>CODEN: JNPRDF</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Amidohydrolases - metabolism ; Aminohydrolases - metabolism ; Anti-Bacterial Agents - chemical synthesis ; Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - pharmacology ; Antibacterial agents ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; Bioconversions. Hemisynthesis ; Biological and medical sciences ; Biotechnology ; Enterococcus faecalis - drug effects ; Enterococcus faecium - drug effects ; Fundamental and applied biological sciences. Psychology ; Lipopeptides ; Medical sciences ; Methicillin Resistance - drug effects ; Methods. Procedures. Technologies ; Microbial Sensitivity Tests ; Micromonosporaceae - enzymology ; Molecular Structure ; Oligopeptides - chemistry ; Peptides, Cyclic - chemical synthesis ; Peptides, Cyclic - chemistry ; Peptides, Cyclic - pharmacology ; Pharmacology. Drug treatments ; Staphylococcus aureus - drug effects ; Tryptophan - chemistry ; Vancomycin Resistance - drug effects</subject><ispartof>Journal of natural products (Washington, D.C.), 2007-03, Vol.70 (3), p.447-450</ispartof><rights>Copyright © 2007 American Chemical Society and American Society of Pharmacognosy</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a381t-b247d85a740c03e40621d485d79d80382a1216640a6b42b2e1561a41db4437353</citedby><cites>FETCH-LOGICAL-a381t-b247d85a740c03e40621d485d79d80382a1216640a6b42b2e1561a41db4437353</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/np068062b$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/np068062b$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2751,27055,27903,27904,56717,56767</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18669762$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17323996$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Curran, William V</creatorcontrib><creatorcontrib>Leese, Richard A</creatorcontrib><creatorcontrib>Jarolmen, Howard</creatorcontrib><creatorcontrib>Borders, Donald B</creatorcontrib><creatorcontrib>Dugourd, Dominique</creatorcontrib><creatorcontrib>Chen, Yuchen</creatorcontrib><creatorcontrib>Cameron, Dale R</creatorcontrib><title>Semisynthetic Approaches to Laspartomycin Analogues</title><title>Journal of natural products (Washington, D.C.)</title><addtitle>J. Nat. Prod</addtitle><description>Laspartomycin C (1), a lipopeptide antibiotic related to amphomycin, consists of a cyclic peptide core and an aspartic acid unit external to the core and linking this to a C15-2,3-unsaturated fatty acid. This was reported initially to be active against Staphylococcus aureus, and more recent studies have shown that it is active against VRE, VISA, and MRSA isolates. The enzymatic cleavage of the fatty acid tail was accomplished with a deacylase produced by Actinoplanes utahensis and resulted in two peptides, designated Peptide 1 and Peptide 2. Semisynthetic derivatives of both peptides have been made, and the principal requirement for biological activity appears to be the presence of an acylaspartic acid.</description><subject>Amidohydrolases - metabolism</subject><subject>Aminohydrolases - metabolism</subject><subject>Anti-Bacterial Agents - chemical synthesis</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antibacterial agents</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Bioconversions. Hemisynthesis</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Enterococcus faecalis - drug effects</subject><subject>Enterococcus faecium - drug effects</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Lipopeptides</subject><subject>Medical sciences</subject><subject>Methicillin Resistance - drug effects</subject><subject>Methods. Procedures. Technologies</subject><subject>Microbial Sensitivity Tests</subject><subject>Micromonosporaceae - enzymology</subject><subject>Molecular Structure</subject><subject>Oligopeptides - chemistry</subject><subject>Peptides, Cyclic - chemical synthesis</subject><subject>Peptides, Cyclic - chemistry</subject><subject>Peptides, Cyclic - pharmacology</subject><subject>Pharmacology. Drug treatments</subject><subject>Staphylococcus aureus - drug effects</subject><subject>Tryptophan - chemistry</subject><subject>Vancomycin Resistance - drug effects</subject><issn>0163-3864</issn><issn>1520-6025</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0M1LwzAYBvAgipvTg_-A7KLgofrmo0l7HJtfMPxgE8RLeJtmrtq1NenA_fdGNraLpxzy48mTh5BTClcUGL2uGpAJSJbtkS6NGUQSWLxPukAlj3giRYccef8JABzS-JB0qOKMp6nsEj6xi8KvqnZu28L0B03jajRz6_tt3R-jb9C19WJliqo_qLCsP5bWH5ODGZbenmzOHnm9vZkO76Px093DcDCOkCe0jTImVJ7EqAQY4FaEgjQXSZyrNE-AJwwpo1IKQJkJljFLY0lR0DwTgise8x65WOeGTt_h3VaHqsaWJVa2XnqtwncUSBHg5RoaV3vv7Ew3rligW2kK-m8hvV0o2LNN6DJb2HwnN5MEcL4B6A2WM4eVKfzOJVKmSrLgorUrfGt_tvfovrRUXMV6-jzRo5cxm76_PerRLheN15_10oU5_T8FfwHvsIbD</recordid><startdate>20070301</startdate><enddate>20070301</enddate><creator>Curran, William V</creator><creator>Leese, Richard A</creator><creator>Jarolmen, Howard</creator><creator>Borders, Donald B</creator><creator>Dugourd, Dominique</creator><creator>Chen, Yuchen</creator><creator>Cameron, Dale R</creator><general>American Chemical Society</general><general>American Society of Pharmacognosy</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>7X8</scope></search><sort><creationdate>20070301</creationdate><title>Semisynthetic Approaches to Laspartomycin Analogues</title><author>Curran, William V ; Leese, Richard A ; Jarolmen, Howard ; Borders, Donald B ; Dugourd, Dominique ; Chen, Yuchen ; Cameron, Dale R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a381t-b247d85a740c03e40621d485d79d80382a1216640a6b42b2e1561a41db4437353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amidohydrolases - metabolism</topic><topic>Aminohydrolases - metabolism</topic><topic>Anti-Bacterial Agents - chemical synthesis</topic><topic>Anti-Bacterial Agents - chemistry</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Antibacterial agents</topic><topic>Antibiotics. Antiinfectious agents. Antiparasitic agents</topic><topic>Bioconversions. Hemisynthesis</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Enterococcus faecalis - drug effects</topic><topic>Enterococcus faecium - drug effects</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Lipopeptides</topic><topic>Medical sciences</topic><topic>Methicillin Resistance - drug effects</topic><topic>Methods. Procedures. Technologies</topic><topic>Microbial Sensitivity Tests</topic><topic>Micromonosporaceae - enzymology</topic><topic>Molecular Structure</topic><topic>Oligopeptides - chemistry</topic><topic>Peptides, Cyclic - chemical synthesis</topic><topic>Peptides, Cyclic - chemistry</topic><topic>Peptides, Cyclic - pharmacology</topic><topic>Pharmacology. Drug treatments</topic><topic>Staphylococcus aureus - drug effects</topic><topic>Tryptophan - chemistry</topic><topic>Vancomycin Resistance - drug effects</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Curran, William V</creatorcontrib><creatorcontrib>Leese, Richard A</creatorcontrib><creatorcontrib>Jarolmen, Howard</creatorcontrib><creatorcontrib>Borders, Donald B</creatorcontrib><creatorcontrib>Dugourd, Dominique</creatorcontrib><creatorcontrib>Chen, Yuchen</creatorcontrib><creatorcontrib>Cameron, Dale R</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>MEDLINE - Academic</collection><jtitle>Journal of natural products (Washington, D.C.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Curran, William V</au><au>Leese, Richard A</au><au>Jarolmen, Howard</au><au>Borders, Donald B</au><au>Dugourd, Dominique</au><au>Chen, Yuchen</au><au>Cameron, Dale R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Semisynthetic Approaches to Laspartomycin Analogues</atitle><jtitle>Journal of natural products (Washington, D.C.)</jtitle><addtitle>J. Nat. Prod</addtitle><date>2007-03-01</date><risdate>2007</risdate><volume>70</volume><issue>3</issue><spage>447</spage><epage>450</epage><pages>447-450</pages><issn>0163-3864</issn><eissn>1520-6025</eissn><coden>JNPRDF</coden><abstract>Laspartomycin C (1), a lipopeptide antibiotic related to amphomycin, consists of a cyclic peptide core and an aspartic acid unit external to the core and linking this to a C15-2,3-unsaturated fatty acid. This was reported initially to be active against Staphylococcus aureus, and more recent studies have shown that it is active against VRE, VISA, and MRSA isolates. The enzymatic cleavage of the fatty acid tail was accomplished with a deacylase produced by Actinoplanes utahensis and resulted in two peptides, designated Peptide 1 and Peptide 2. Semisynthetic derivatives of both peptides have been made, and the principal requirement for biological activity appears to be the presence of an acylaspartic acid.</abstract><cop>Washington, DC</cop><cop>Glendale, AZ</cop><pub>American Chemical Society</pub><pmid>17323996</pmid><doi>10.1021/np068062b</doi><tpages>4</tpages></addata></record> |
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| subjects | Amidohydrolases - metabolism Aminohydrolases - metabolism Anti-Bacterial Agents - chemical synthesis Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - pharmacology Antibacterial agents Antibiotics. Antiinfectious agents. Antiparasitic agents Bioconversions. Hemisynthesis Biological and medical sciences Biotechnology Enterococcus faecalis - drug effects Enterococcus faecium - drug effects Fundamental and applied biological sciences. Psychology Lipopeptides Medical sciences Methicillin Resistance - drug effects Methods. Procedures. Technologies Microbial Sensitivity Tests Micromonosporaceae - enzymology Molecular Structure Oligopeptides - chemistry Peptides, Cyclic - chemical synthesis Peptides, Cyclic - chemistry Peptides, Cyclic - pharmacology Pharmacology. Drug treatments Staphylococcus aureus - drug effects Tryptophan - chemistry Vancomycin Resistance - drug effects |
| title | Semisynthetic Approaches to Laspartomycin Analogues |
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