Chemically Diverse Helix-Constrained Peptides Using Selenocysteine Crosslinking
The use of selenocysteines and various cross-linkers to induce helicity in a bioactive peptide is described. The higher reactivity of selenocysteine, relative to cysteine, facilitates rapid cross-linking within unprotected linear peptides under mild aqueous conditions. Alkylating agents of variable...
Gespeichert in:
| Veröffentlicht in: | Organic letters 2018-03, Vol.20 (5), p.1453-1456 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1456 |
|---|---|
| container_issue | 5 |
| container_start_page | 1453 |
| container_title | Organic letters |
| container_volume | 20 |
| creator | Dantas de Araujo, Aline Perry, Samuel R Fairlie, David P |
| description | The use of selenocysteines and various cross-linkers to induce helicity in a bioactive peptide is described. The higher reactivity of selenocysteine, relative to cysteine, facilitates rapid cross-linking within unprotected linear peptides under mild aqueous conditions. Alkylating agents of variable topology and electrophilicity were used to link pairs of selenocysteines within a p53 peptide. Facile selenoether formation enables diverse tailoring of the helical peptide structure. |
| doi_str_mv | 10.1021/acs.orglett.8b00233 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2007120200</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2007120200</sourcerecordid><originalsourceid>FETCH-LOGICAL-a345t-7c2dc9cbbe05903ad083cc0bad632b0f3d8fdf3aa446f1d83e5d58183ab8d0763</originalsourceid><addsrcrecordid>eNp9kMtOwzAQRS0EoqXwBUgoSzZpx3ZeXaLwKFKlIkHXkWNPiouTFDtB9O9x1cCS1Yxm7p3HIeSawpQCozMh3bS1G4NdN81KAMb5CRnTmPEwhZid_uUJjMiFc1sA6ivzczJi8yihkCRjssrfsdZSGLMP7vUXWofBAo3-DvO2cZ0VukEVvOCu0wpdsHa62QSvaLBp5d516NtBblvnjG4-fO-SnFXCOLwa4oSsHx_e8kW4XD0953fLUPAo7sJUMiXnsiwR4jlwoSDjUkIpVMJZCRVXWaUqLkQUJRVVGcdYxRnNuCgzBWnCJ-T2OHdn288eXVfU2kk0RjTY9q5gACll4IOX8qNUHu60WBU7q2th9wWF4kCy8CSLgWQxkPSum2FBX9ao_jy_6LxgdhQc3Nu2t43_99-RP-1og9U</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2007120200</pqid></control><display><type>article</type><title>Chemically Diverse Helix-Constrained Peptides Using Selenocysteine Crosslinking</title><source>MEDLINE</source><source>ACS Publications</source><creator>Dantas de Araujo, Aline ; Perry, Samuel R ; Fairlie, David P</creator><creatorcontrib>Dantas de Araujo, Aline ; Perry, Samuel R ; Fairlie, David P</creatorcontrib><description>The use of selenocysteines and various cross-linkers to induce helicity in a bioactive peptide is described. The higher reactivity of selenocysteine, relative to cysteine, facilitates rapid cross-linking within unprotected linear peptides under mild aqueous conditions. Alkylating agents of variable topology and electrophilicity were used to link pairs of selenocysteines within a p53 peptide. Facile selenoether formation enables diverse tailoring of the helical peptide structure.</description><identifier>ISSN: 1523-7060</identifier><identifier>EISSN: 1523-7052</identifier><identifier>DOI: 10.1021/acs.orglett.8b00233</identifier><identifier>PMID: 29461066</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Alkylation ; Antineoplastic Agents - chemistry ; Antineoplastic Agents - pharmacology ; Binding Sites ; Cell Survival ; Cross-Linking Reagents - chemistry ; Humans ; MCF-7 Cells ; Molecular Structure ; Peptides - chemistry ; Peptides - pharmacology ; Protein Binding ; Protein Conformation ; Selenocysteine - chemistry ; Stereoisomerism ; Surface Properties ; Water</subject><ispartof>Organic letters, 2018-03, Vol.20 (5), p.1453-1456</ispartof><rights>Copyright © 2018 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a345t-7c2dc9cbbe05903ad083cc0bad632b0f3d8fdf3aa446f1d83e5d58183ab8d0763</citedby><cites>FETCH-LOGICAL-a345t-7c2dc9cbbe05903ad083cc0bad632b0f3d8fdf3aa446f1d83e5d58183ab8d0763</cites><orcidid>0000-0002-7856-8566</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acs.orglett.8b00233$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.orglett.8b00233$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29461066$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dantas de Araujo, Aline</creatorcontrib><creatorcontrib>Perry, Samuel R</creatorcontrib><creatorcontrib>Fairlie, David P</creatorcontrib><title>Chemically Diverse Helix-Constrained Peptides Using Selenocysteine Crosslinking</title><title>Organic letters</title><addtitle>Org. Lett</addtitle><description>The use of selenocysteines and various cross-linkers to induce helicity in a bioactive peptide is described. The higher reactivity of selenocysteine, relative to cysteine, facilitates rapid cross-linking within unprotected linear peptides under mild aqueous conditions. Alkylating agents of variable topology and electrophilicity were used to link pairs of selenocysteines within a p53 peptide. Facile selenoether formation enables diverse tailoring of the helical peptide structure.</description><subject>Alkylation</subject><subject>Antineoplastic Agents - chemistry</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>Binding Sites</subject><subject>Cell Survival</subject><subject>Cross-Linking Reagents - chemistry</subject><subject>Humans</subject><subject>MCF-7 Cells</subject><subject>Molecular Structure</subject><subject>Peptides - chemistry</subject><subject>Peptides - pharmacology</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Selenocysteine - chemistry</subject><subject>Stereoisomerism</subject><subject>Surface Properties</subject><subject>Water</subject><issn>1523-7060</issn><issn>1523-7052</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtOwzAQRS0EoqXwBUgoSzZpx3ZeXaLwKFKlIkHXkWNPiouTFDtB9O9x1cCS1Yxm7p3HIeSawpQCozMh3bS1G4NdN81KAMb5CRnTmPEwhZid_uUJjMiFc1sA6ivzczJi8yihkCRjssrfsdZSGLMP7vUXWofBAo3-DvO2cZ0VukEVvOCu0wpdsHa62QSvaLBp5d516NtBblvnjG4-fO-SnFXCOLwa4oSsHx_e8kW4XD0953fLUPAo7sJUMiXnsiwR4jlwoSDjUkIpVMJZCRVXWaUqLkQUJRVVGcdYxRnNuCgzBWnCJ-T2OHdn288eXVfU2kk0RjTY9q5gACll4IOX8qNUHu60WBU7q2th9wWF4kCy8CSLgWQxkPSum2FBX9ao_jy_6LxgdhQc3Nu2t43_99-RP-1og9U</recordid><startdate>20180302</startdate><enddate>20180302</enddate><creator>Dantas de Araujo, Aline</creator><creator>Perry, Samuel R</creator><creator>Fairlie, David P</creator><general>American Chemical Society</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>7X8</scope><orcidid>https://orcid.org/0000-0002-7856-8566</orcidid></search><sort><creationdate>20180302</creationdate><title>Chemically Diverse Helix-Constrained Peptides Using Selenocysteine Crosslinking</title><author>Dantas de Araujo, Aline ; Perry, Samuel R ; Fairlie, David P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a345t-7c2dc9cbbe05903ad083cc0bad632b0f3d8fdf3aa446f1d83e5d58183ab8d0763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Alkylation</topic><topic>Antineoplastic Agents - chemistry</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>Binding Sites</topic><topic>Cell Survival</topic><topic>Cross-Linking Reagents - chemistry</topic><topic>Humans</topic><topic>MCF-7 Cells</topic><topic>Molecular Structure</topic><topic>Peptides - chemistry</topic><topic>Peptides - pharmacology</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Selenocysteine - chemistry</topic><topic>Stereoisomerism</topic><topic>Surface Properties</topic><topic>Water</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dantas de Araujo, Aline</creatorcontrib><creatorcontrib>Perry, Samuel R</creatorcontrib><creatorcontrib>Fairlie, David 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>MEDLINE - Academic</collection><jtitle>Organic letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dantas de Araujo, Aline</au><au>Perry, Samuel R</au><au>Fairlie, David P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chemically Diverse Helix-Constrained Peptides Using Selenocysteine Crosslinking</atitle><jtitle>Organic letters</jtitle><addtitle>Org. Lett</addtitle><date>2018-03-02</date><risdate>2018</risdate><volume>20</volume><issue>5</issue><spage>1453</spage><epage>1456</epage><pages>1453-1456</pages><issn>1523-7060</issn><eissn>1523-7052</eissn><abstract>The use of selenocysteines and various cross-linkers to induce helicity in a bioactive peptide is described. The higher reactivity of selenocysteine, relative to cysteine, facilitates rapid cross-linking within unprotected linear peptides under mild aqueous conditions. Alkylating agents of variable topology and electrophilicity were used to link pairs of selenocysteines within a p53 peptide. Facile selenoether formation enables diverse tailoring of the helical peptide structure.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>29461066</pmid><doi>10.1021/acs.orglett.8b00233</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0002-7856-8566</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1523-7060 |
| ispartof | Organic letters, 2018-03, Vol.20 (5), p.1453-1456 |
| issn | 1523-7060 1523-7052 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2007120200 |
| source | MEDLINE; ACS Publications |
| subjects | Alkylation Antineoplastic Agents - chemistry Antineoplastic Agents - pharmacology Binding Sites Cell Survival Cross-Linking Reagents - chemistry Humans MCF-7 Cells Molecular Structure Peptides - chemistry Peptides - pharmacology Protein Binding Protein Conformation Selenocysteine - chemistry Stereoisomerism Surface Properties Water |
| title | Chemically Diverse Helix-Constrained Peptides Using Selenocysteine Crosslinking |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T03%3A18%3A34IST&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=Chemically%20Diverse%20Helix-Constrained%20Peptides%20Using%20Selenocysteine%20Crosslinking&rft.jtitle=Organic%20letters&rft.au=Dantas%20de%20Araujo,%20Aline&rft.date=2018-03-02&rft.volume=20&rft.issue=5&rft.spage=1453&rft.epage=1456&rft.pages=1453-1456&rft.issn=1523-7060&rft.eissn=1523-7052&rft_id=info:doi/10.1021/acs.orglett.8b00233&rft_dat=%3Cproquest_cross%3E2007120200%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=2007120200&rft_id=info:pmid/29461066&rfr_iscdi=true |