Rapid and Selective Chemical Editing of Ribosomally Synthesized and Post‐Translationally Modified Peptides (RiPPs) via CuII‐Catalyzed β‐Borylation of Dehydroamino Acids
We report the fast and selective chemical editing of ribosomally synthesized and post‐translationally modified peptides (RiPPs) by β‐borylation of dehydroalanine (Dha) residues. The thiopeptide thiostrepton was modified efficiently using CuII‐catalysis under mild conditions and 1D/2D NMR of the puri...
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| Veröffentlicht in: | Angewandte Chemie 2021-02, Vol.133 (8), p.3992-3996 |
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| creator | Vries, Reinder H. Viel, Jakob H. Kuipers, Oscar P. Roelfes, Gerard |
| description | We report the fast and selective chemical editing of ribosomally synthesized and post‐translationally modified peptides (RiPPs) by β‐borylation of dehydroalanine (Dha) residues. The thiopeptide thiostrepton was modified efficiently using CuII‐catalysis under mild conditions and 1D/2D NMR of the purified product showed site‐selective borylation of the terminal Dha residues. Using similar conditions, the thiopeptide nosiheptide, lanthipeptide nisin Z, and protein SUMO_G98Dha were also modified efficiently. Borylated thiostrepton showed an up to 84‐fold increase in water solubility, and minimum inhibitory concentration (MIC) assays showed that antimicrobial activity was maintained in thiostrepton and nosiheptide. The introduced boronic‐acid functionalities were shown to be valuable handles for chemical mutagenesis and in a reversible click reaction with triols for the pH‐controlled labeling of RiPPs.
Dehydroamino‐acid‐containing natural peptides and proteins were rapidly and selectively borylated at the β‐position using copper(II) catalysis. The introduced boronic‐acid functionalities are valuable handles for chemical mutagenesis and, in a reversible click reaction with triols, for the pH‐controlled labeling of ribosomally synthesized and post‐translationally modified peptides (RiPPs). |
| doi_str_mv | 10.1002/ange.202011460 |
| format | Article |
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Dehydroamino‐acid‐containing natural peptides and proteins were rapidly and selectively borylated at the β‐position using copper(II) catalysis. The introduced boronic‐acid functionalities are valuable handles for chemical mutagenesis and, in a reversible click reaction with triols, for the pH‐controlled labeling of ribosomally synthesized and post‐translationally modified peptides (RiPPs).</description><identifier>ISSN: 0044-8249</identifier><identifier>EISSN: 1521-3757</identifier><identifier>DOI: 10.1002/ange.202011460</identifier><language>eng</language><publisher>Weinheim: Wiley Subscription Services, Inc</publisher><subject>Antiinfectives and antibacterials ; Antimicrobial activity ; Catalysis ; Chemical reactions ; Chemical synthesis ; Chemistry ; dehydroalanine ; Editing ; late-stage chemical editing ; Minimum inhibitory concentration ; Mutagenesis ; Nisin ; NMR ; Nosiheptide ; Nuclear magnetic resonance ; peptide modification ; Peptides ; Residues ; RiPPs ; Thiostrepton ; Triols ; β-borylation</subject><ispartof>Angewandte Chemie, 2021-02, Vol.133 (8), p.3992-3996</ispartof><rights>2020 The Authors. Angewandte Chemie published by Wiley-VCH GmbH</rights><rights>2020. This article is published under http://creativecommons.org/licenses/by-nc/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0002-0364-9564 ; 0000-0001-5596-7735</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fange.202011460$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fange.202011460$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1416,27923,27924,45573,45574</link.rule.ids></links><search><creatorcontrib>Vries, Reinder H.</creatorcontrib><creatorcontrib>Viel, Jakob H.</creatorcontrib><creatorcontrib>Kuipers, Oscar P.</creatorcontrib><creatorcontrib>Roelfes, Gerard</creatorcontrib><title>Rapid and Selective Chemical Editing of Ribosomally Synthesized and Post‐Translationally Modified Peptides (RiPPs) via CuII‐Catalyzed β‐Borylation of Dehydroamino Acids</title><title>Angewandte Chemie</title><description>We report the fast and selective chemical editing of ribosomally synthesized and post‐translationally modified peptides (RiPPs) by β‐borylation of dehydroalanine (Dha) residues. The thiopeptide thiostrepton was modified efficiently using CuII‐catalysis under mild conditions and 1D/2D NMR of the purified product showed site‐selective borylation of the terminal Dha residues. Using similar conditions, the thiopeptide nosiheptide, lanthipeptide nisin Z, and protein SUMO_G98Dha were also modified efficiently. Borylated thiostrepton showed an up to 84‐fold increase in water solubility, and minimum inhibitory concentration (MIC) assays showed that antimicrobial activity was maintained in thiostrepton and nosiheptide. The introduced boronic‐acid functionalities were shown to be valuable handles for chemical mutagenesis and in a reversible click reaction with triols for the pH‐controlled labeling of RiPPs.
Dehydroamino‐acid‐containing natural peptides and proteins were rapidly and selectively borylated at the β‐position using copper(II) catalysis. The introduced boronic‐acid functionalities are valuable handles for chemical mutagenesis and, in a reversible click reaction with triols, for the pH‐controlled labeling of ribosomally synthesized and post‐translationally modified peptides (RiPPs).</description><subject>Antiinfectives and antibacterials</subject><subject>Antimicrobial activity</subject><subject>Catalysis</subject><subject>Chemical reactions</subject><subject>Chemical synthesis</subject><subject>Chemistry</subject><subject>dehydroalanine</subject><subject>Editing</subject><subject>late-stage chemical editing</subject><subject>Minimum inhibitory concentration</subject><subject>Mutagenesis</subject><subject>Nisin</subject><subject>NMR</subject><subject>Nosiheptide</subject><subject>Nuclear magnetic resonance</subject><subject>peptide modification</subject><subject>Peptides</subject><subject>Residues</subject><subject>RiPPs</subject><subject>Thiostrepton</subject><subject>Triols</subject><subject>β-borylation</subject><issn>0044-8249</issn><issn>1521-3757</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><recordid>eNo9kc1u00AUhUcIJELptuuR2MDC7Z0f2-NlMKFEammUtmtr7LlubuV4jMcpMisegTdB6oPwEDxJHYK6ujrSd87R1WHsRMCpAJBntr3DUwkShNAJvGAzEUsRqTROX7IZgNaRkTp7zd6EcA8AiUyzGfu9th05blvHr7HBaqAH5PkGt1TZhi8cDdTecV_zNZU--K1tmpFfj-2wwUA_8OBc-TD8_fnrprdtaOxAvv2HXXpHNU3MCruBHAb-fk2rVfjAH8jyfLdcTqbcDrYZ90l_Hif50ffjIWJf-gk3o-u93VLr-bwiF96yV7VtAh7_v0fs9vPiJv8SXVydL_P5RdQJYSBKRZnFWAOCUkormTitDMRJXTlVQlpam2IltE3SREhnJSaJ0GVt4ipzJjOgjti7Q27X-287DENx73f99FcopDYmVlqkZqKyA_WdGhyLrqet7cdCQLFfpNgvUjwvUsy_ni-elXoCluaHpA</recordid><startdate>20210219</startdate><enddate>20210219</enddate><creator>Vries, Reinder H.</creator><creator>Viel, Jakob H.</creator><creator>Kuipers, Oscar P.</creator><creator>Roelfes, Gerard</creator><general>Wiley Subscription Services, Inc</general><scope>24P</scope><scope>WIN</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><orcidid>https://orcid.org/0000-0002-0364-9564</orcidid><orcidid>https://orcid.org/0000-0001-5596-7735</orcidid></search><sort><creationdate>20210219</creationdate><title>Rapid and Selective Chemical Editing of Ribosomally Synthesized and Post‐Translationally Modified Peptides (RiPPs) via CuII‐Catalyzed β‐Borylation of Dehydroamino Acids</title><author>Vries, Reinder H. ; Viel, Jakob H. ; Kuipers, Oscar P. ; Roelfes, Gerard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p1180-71b95ef0e03334326d438056fcd3b07baa7ec14a67612da2e6614bf85c9d89803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Antiinfectives and antibacterials</topic><topic>Antimicrobial activity</topic><topic>Catalysis</topic><topic>Chemical reactions</topic><topic>Chemical synthesis</topic><topic>Chemistry</topic><topic>dehydroalanine</topic><topic>Editing</topic><topic>late-stage chemical editing</topic><topic>Minimum inhibitory concentration</topic><topic>Mutagenesis</topic><topic>Nisin</topic><topic>NMR</topic><topic>Nosiheptide</topic><topic>Nuclear magnetic resonance</topic><topic>peptide modification</topic><topic>Peptides</topic><topic>Residues</topic><topic>RiPPs</topic><topic>Thiostrepton</topic><topic>Triols</topic><topic>β-borylation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vries, Reinder H.</creatorcontrib><creatorcontrib>Viel, Jakob H.</creatorcontrib><creatorcontrib>Kuipers, Oscar P.</creatorcontrib><creatorcontrib>Roelfes, Gerard</creatorcontrib><collection>Wiley-Blackwell Open Access Titles</collection><collection>Wiley Free Content</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>Angewandte Chemie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vries, Reinder H.</au><au>Viel, Jakob H.</au><au>Kuipers, Oscar P.</au><au>Roelfes, Gerard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rapid and Selective Chemical Editing of Ribosomally Synthesized and Post‐Translationally Modified Peptides (RiPPs) via CuII‐Catalyzed β‐Borylation of Dehydroamino Acids</atitle><jtitle>Angewandte Chemie</jtitle><date>2021-02-19</date><risdate>2021</risdate><volume>133</volume><issue>8</issue><spage>3992</spage><epage>3996</epage><pages>3992-3996</pages><issn>0044-8249</issn><eissn>1521-3757</eissn><abstract>We report the fast and selective chemical editing of ribosomally synthesized and post‐translationally modified peptides (RiPPs) by β‐borylation of dehydroalanine (Dha) residues. The thiopeptide thiostrepton was modified efficiently using CuII‐catalysis under mild conditions and 1D/2D NMR of the purified product showed site‐selective borylation of the terminal Dha residues. Using similar conditions, the thiopeptide nosiheptide, lanthipeptide nisin Z, and protein SUMO_G98Dha were also modified efficiently. Borylated thiostrepton showed an up to 84‐fold increase in water solubility, and minimum inhibitory concentration (MIC) assays showed that antimicrobial activity was maintained in thiostrepton and nosiheptide. The introduced boronic‐acid functionalities were shown to be valuable handles for chemical mutagenesis and in a reversible click reaction with triols for the pH‐controlled labeling of RiPPs.
Dehydroamino‐acid‐containing natural peptides and proteins were rapidly and selectively borylated at the β‐position using copper(II) catalysis. The introduced boronic‐acid functionalities are valuable handles for chemical mutagenesis and, in a reversible click reaction with triols, for the pH‐controlled labeling of ribosomally synthesized and post‐translationally modified peptides (RiPPs).</abstract><cop>Weinheim</cop><pub>Wiley Subscription Services, Inc</pub><doi>10.1002/ange.202011460</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0002-0364-9564</orcidid><orcidid>https://orcid.org/0000-0001-5596-7735</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Antiinfectives and antibacterials Antimicrobial activity Catalysis Chemical reactions Chemical synthesis Chemistry dehydroalanine Editing late-stage chemical editing Minimum inhibitory concentration Mutagenesis Nisin NMR Nosiheptide Nuclear magnetic resonance peptide modification Peptides Residues RiPPs Thiostrepton Triols β-borylation |
| title | Rapid and Selective Chemical Editing of Ribosomally Synthesized and Post‐Translationally Modified Peptides (RiPPs) via CuII‐Catalyzed β‐Borylation of Dehydroamino Acids |
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