Novel chemical probes for the investigation of nonribosomal peptide assembly
Chemical probes were devised and evaluated for the capture of biosynthetic intermediates involved in the bio-assembly of the nonribosomal peptide echinomycin. Putative intermediate peptide species were isolated and characterised, providing fresh insights into pathway substrate flexibility and paving...
Gespeichert in:
| Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2017, Vol.53 (52), p.7088-7091 |
|---|---|
| Hauptverfasser: | , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 7091 |
|---|---|
| container_issue | 52 |
| container_start_page | 7088 |
| container_title | Chemical communications (Cambridge, England) |
| container_volume | 53 |
| creator | Ho, Y T Candace Leng, Daniel J Ghiringhelli, Francesca Wilkening, Ina Bushell, Dexter P Kostner, Otto Riva, Elena Havemann, Judith Passarella, Daniele Tosin, Manuela |
| description | Chemical probes were devised and evaluated for the capture of biosynthetic intermediates involved in the bio-assembly of the nonribosomal peptide echinomycin. Putative intermediate peptide species were isolated and characterised, providing fresh insights into pathway substrate flexibility and paving the way for novel chemoenzymatic approaches towards unnatural peptides. |
| doi_str_mv | 10.1039/c7cc02427d |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1925880471</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1911208964</sourcerecordid><originalsourceid>FETCH-LOGICAL-c422t-aa629fbbeef75181582acab21a4b3b3e55f6a3eb79ee635d6cceb926202760023</originalsourceid><addsrcrecordid>eNqNkEtLxDAUhYMojo5u_AGSpQjVvJMupT5h0I2Cu5Kkt06kbcamMzD_3o4zuvZuzl18HD4OQmeUXFHC82uvvSdMMF3toSPKlcikMO_7m1_mmeZCTtBxSp9kPCrNIZowo5iWzByh2XNcQYP9HNrgbYMXfXSQcB17PMwBh24FaQgfdgixw7HGXez64GKK7QaGxRAqwDYlaF2zPkEHtW0SnO5yit7u716Lx2z28vBU3MwyLxgbMmsVy2vnAGotqRmVmPXWMWqF446DlLWyHJzOARSXlfIeXM4UI0wrQhifoott72j7tRwFyzYkD01jO4jLVNKcSWOI0PQfKKWMmFyJEb3cor6PKfVQl4s-tLZfl5SUm6HLQhfFz9C3I3y-6126Fqo_9HdZ_g20mnkF</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1911208964</pqid></control><display><type>article</type><title>Novel chemical probes for the investigation of nonribosomal peptide assembly</title><source>MEDLINE</source><source>Royal Society Of Chemistry Journals 2008-</source><source>Alma/SFX Local Collection</source><creator>Ho, Y T Candace ; Leng, Daniel J ; Ghiringhelli, Francesca ; Wilkening, Ina ; Bushell, Dexter P ; Kostner, Otto ; Riva, Elena ; Havemann, Judith ; Passarella, Daniele ; Tosin, Manuela</creator><creatorcontrib>Ho, Y T Candace ; Leng, Daniel J ; Ghiringhelli, Francesca ; Wilkening, Ina ; Bushell, Dexter P ; Kostner, Otto ; Riva, Elena ; Havemann, Judith ; Passarella, Daniele ; Tosin, Manuela</creatorcontrib><description>Chemical probes were devised and evaluated for the capture of biosynthetic intermediates involved in the bio-assembly of the nonribosomal peptide echinomycin. Putative intermediate peptide species were isolated and characterised, providing fresh insights into pathway substrate flexibility and paving the way for novel chemoenzymatic approaches towards unnatural peptides.</description><identifier>ISSN: 1359-7345</identifier><identifier>EISSN: 1364-548X</identifier><identifier>DOI: 10.1039/c7cc02427d</identifier><identifier>PMID: 28627528</identifier><language>eng</language><publisher>England</publisher><subject>Assembly ; Echinomycin - biosynthesis ; Echinomycin - chemistry ; Flexibility ; Molecular Probes - analysis ; Molecular Probes - chemistry ; Molecular Structure ; Pathways ; Paving ; Peptides ; Substrates</subject><ispartof>Chemical communications (Cambridge, England), 2017, Vol.53 (52), p.7088-7091</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c422t-aa629fbbeef75181582acab21a4b3b3e55f6a3eb79ee635d6cceb926202760023</citedby><cites>FETCH-LOGICAL-c422t-aa629fbbeef75181582acab21a4b3b3e55f6a3eb79ee635d6cceb926202760023</cites><orcidid>0000-0003-4340-9431 ; 0000-0001-6180-9581</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4022,27922,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28627528$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ho, Y T Candace</creatorcontrib><creatorcontrib>Leng, Daniel J</creatorcontrib><creatorcontrib>Ghiringhelli, Francesca</creatorcontrib><creatorcontrib>Wilkening, Ina</creatorcontrib><creatorcontrib>Bushell, Dexter P</creatorcontrib><creatorcontrib>Kostner, Otto</creatorcontrib><creatorcontrib>Riva, Elena</creatorcontrib><creatorcontrib>Havemann, Judith</creatorcontrib><creatorcontrib>Passarella, Daniele</creatorcontrib><creatorcontrib>Tosin, Manuela</creatorcontrib><title>Novel chemical probes for the investigation of nonribosomal peptide assembly</title><title>Chemical communications (Cambridge, England)</title><addtitle>Chem Commun (Camb)</addtitle><description>Chemical probes were devised and evaluated for the capture of biosynthetic intermediates involved in the bio-assembly of the nonribosomal peptide echinomycin. Putative intermediate peptide species were isolated and characterised, providing fresh insights into pathway substrate flexibility and paving the way for novel chemoenzymatic approaches towards unnatural peptides.</description><subject>Assembly</subject><subject>Echinomycin - biosynthesis</subject><subject>Echinomycin - chemistry</subject><subject>Flexibility</subject><subject>Molecular Probes - analysis</subject><subject>Molecular Probes - chemistry</subject><subject>Molecular Structure</subject><subject>Pathways</subject><subject>Paving</subject><subject>Peptides</subject><subject>Substrates</subject><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEtLxDAUhYMojo5u_AGSpQjVvJMupT5h0I2Cu5Kkt06kbcamMzD_3o4zuvZuzl18HD4OQmeUXFHC82uvvSdMMF3toSPKlcikMO_7m1_mmeZCTtBxSp9kPCrNIZowo5iWzByh2XNcQYP9HNrgbYMXfXSQcB17PMwBh24FaQgfdgixw7HGXez64GKK7QaGxRAqwDYlaF2zPkEHtW0SnO5yit7u716Lx2z28vBU3MwyLxgbMmsVy2vnAGotqRmVmPXWMWqF446DlLWyHJzOARSXlfIeXM4UI0wrQhifoott72j7tRwFyzYkD01jO4jLVNKcSWOI0PQfKKWMmFyJEb3cor6PKfVQl4s-tLZfl5SUm6HLQhfFz9C3I3y-6126Fqo_9HdZ_g20mnkF</recordid><startdate>2017</startdate><enddate>2017</enddate><creator>Ho, Y T Candace</creator><creator>Leng, Daniel J</creator><creator>Ghiringhelli, Francesca</creator><creator>Wilkening, Ina</creator><creator>Bushell, Dexter P</creator><creator>Kostner, Otto</creator><creator>Riva, Elena</creator><creator>Havemann, Judith</creator><creator>Passarella, Daniele</creator><creator>Tosin, Manuela</creator><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><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><orcidid>https://orcid.org/0000-0003-4340-9431</orcidid><orcidid>https://orcid.org/0000-0001-6180-9581</orcidid></search><sort><creationdate>2017</creationdate><title>Novel chemical probes for the investigation of nonribosomal peptide assembly</title><author>Ho, Y T Candace ; Leng, Daniel J ; Ghiringhelli, Francesca ; Wilkening, Ina ; Bushell, Dexter P ; Kostner, Otto ; Riva, Elena ; Havemann, Judith ; Passarella, Daniele ; Tosin, Manuela</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c422t-aa629fbbeef75181582acab21a4b3b3e55f6a3eb79ee635d6cceb926202760023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Assembly</topic><topic>Echinomycin - biosynthesis</topic><topic>Echinomycin - chemistry</topic><topic>Flexibility</topic><topic>Molecular Probes - analysis</topic><topic>Molecular Probes - chemistry</topic><topic>Molecular Structure</topic><topic>Pathways</topic><topic>Paving</topic><topic>Peptides</topic><topic>Substrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ho, Y T Candace</creatorcontrib><creatorcontrib>Leng, Daniel J</creatorcontrib><creatorcontrib>Ghiringhelli, Francesca</creatorcontrib><creatorcontrib>Wilkening, Ina</creatorcontrib><creatorcontrib>Bushell, Dexter P</creatorcontrib><creatorcontrib>Kostner, Otto</creatorcontrib><creatorcontrib>Riva, Elena</creatorcontrib><creatorcontrib>Havemann, Judith</creatorcontrib><creatorcontrib>Passarella, Daniele</creatorcontrib><creatorcontrib>Tosin, Manuela</creatorcontrib><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><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Chemical communications (Cambridge, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ho, Y T Candace</au><au>Leng, Daniel J</au><au>Ghiringhelli, Francesca</au><au>Wilkening, Ina</au><au>Bushell, Dexter P</au><au>Kostner, Otto</au><au>Riva, Elena</au><au>Havemann, Judith</au><au>Passarella, Daniele</au><au>Tosin, Manuela</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Novel chemical probes for the investigation of nonribosomal peptide assembly</atitle><jtitle>Chemical communications (Cambridge, England)</jtitle><addtitle>Chem Commun (Camb)</addtitle><date>2017</date><risdate>2017</risdate><volume>53</volume><issue>52</issue><spage>7088</spage><epage>7091</epage><pages>7088-7091</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>Chemical probes were devised and evaluated for the capture of biosynthetic intermediates involved in the bio-assembly of the nonribosomal peptide echinomycin. Putative intermediate peptide species were isolated and characterised, providing fresh insights into pathway substrate flexibility and paving the way for novel chemoenzymatic approaches towards unnatural peptides.</abstract><cop>England</cop><pmid>28627528</pmid><doi>10.1039/c7cc02427d</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0003-4340-9431</orcidid><orcidid>https://orcid.org/0000-0001-6180-9581</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1359-7345 |
| ispartof | Chemical communications (Cambridge, England), 2017, Vol.53 (52), p.7088-7091 |
| issn | 1359-7345 1364-548X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1925880471 |
| source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Assembly Echinomycin - biosynthesis Echinomycin - chemistry Flexibility Molecular Probes - analysis Molecular Probes - chemistry Molecular Structure Pathways Paving Peptides Substrates |
| title | Novel chemical probes for the investigation of nonribosomal peptide assembly |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-11T21%3A57%3A13IST&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=Novel%20chemical%20probes%20for%20the%20investigation%20of%20nonribosomal%20peptide%20assembly&rft.jtitle=Chemical%20communications%20(Cambridge,%20England)&rft.au=Ho,%20Y%20T%20Candace&rft.date=2017&rft.volume=53&rft.issue=52&rft.spage=7088&rft.epage=7091&rft.pages=7088-7091&rft.issn=1359-7345&rft.eissn=1364-548X&rft_id=info:doi/10.1039/c7cc02427d&rft_dat=%3Cproquest_cross%3E1911208964%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=1911208964&rft_id=info:pmid/28627528&rfr_iscdi=true |