Triphosgene: an efficient carbonylating agent for liquid and solid‐phase aza‐peptide synthesis. Application to the synthesis of two aza‐analogues of the AChR MIR decapeptide
Identifieur interne : 000A28 ( Istex/Corpus ); précédent : 000A27; suivant : 000A29Triphosgene: an efficient carbonylating agent for liquid and solid‐phase aza‐peptide synthesis. Application to the synthesis of two aza‐analogues of the AChR MIR decapeptide
Auteurs : Frédéric André ; Michel Marraud ; Theodoros Tsouloufis ; Socrates J. Tzartos ; Guy BoussardSource :
- Journal of Peptide Science [ 1075-2617 ] ; 1997-11.
English descriptors
- KwdEn :
- Achr, Acoetape, Acoetape mixture, Amide, Amino, Amino compound, Aqueous khso4, Azasn, Azasn residue, Carbazic, Carbazic acid chloride, Cdcl3, Cgh2, Chem, Crude material, Derivative, Eluent, Ester, Ethanolic solution, European peptide society, Filtration, Gradual return, Gravity silica, Hplc, Human achr, Hydrazine, Iprohadcm, John wiley sons, Main immunogenic region, Organic phase, Peptide, Peptide chain, Peptide science, Perkin trans, Phosgene, Procbh2, Procbh2 cgh2, Progressive return, Room temperature, Triphosgene.
- Teeft :
- Achr, Acoetape, Acoetape mixture, Amide, Amino, Amino compound, Aqueous khso4, Azasn, Azasn residue, Carbazic, Carbazic acid chloride, Cdcl3, Cgh2, Chem, Crude material, Derivative, Eluent, Ester, Ethanolic solution, European peptide society, Filtration, Gradual return, Gravity silica, Hplc, Human achr, Hydrazine, Iprohadcm, John wiley sons, Main immunogenic region, Organic phase, Peptide, Peptide chain, Peptide science, Perkin trans, Phosgene, Procbh2, Procbh2 cgh2, Progressive return, Room temperature, Triphosgene.
Abstract
The Nα/CαH exchange in aza‐peptides has the advantage of preserving the side chain. Bis(trichloromethyl)carbonate or triphosgene is a solid, stable phosgene substitute which retains its high reactivity. Temperature and coupling times are greatly reduced with reference to other usually recommended carbonylating agents, while purity and yield are increased. It has been used, in both liquid‐ and solid‐phase procedures, for the synthesis of various aza‐analogues of dipeptides, tripeptides and decapeptides containing the alanine, aspartic acid and asparagine aza‐residue. ©1997 European Peptide Society and John Wiley & Sons, Ltd.
Url:
DOI: 10.1002/(SICI)1099-1387(199711)3:6<429::AID-PSC115>3.0.CO;2-C
Links to Exploration step
ISTEX:8272C873EB148DD4AD01D56B5DA4DA5541D4FBAFLe document en format XML
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Tzartos</name><affiliations><json:string>Hellenic Pasteur Institute, Athens, Greece</json:string></affiliations></json:item><json:item><name>Guy Boussard</name><affiliations><json:string>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>aza‐alanine</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>aza‐asparagine</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>aza‐aspartic acid</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>aza‐peptides</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>triphosgene</value></json:item></subject><articleId><json:string>PSC115</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>The Nα/CαH exchange in aza‐peptides has the advantage of preserving the side chain. 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It has been used, in both liquid‐ and solid‐phase procedures, for the synthesis of various aza‐analogues of dipeptides, tripeptides and decapeptides containing the alanine, aspartic acid and asparagine aza‐residue. ©1997 European Peptide Society and John Wiley & Sons, Ltd.</abstract><qualityIndicators><score>6.044</score><pdfVersion>1.2</pdfVersion><pdfPageSize>595 x 842 pts (A4)</pdfPageSize><refBibsNative>true</refBibsNative><abstractCharCount>631</abstractCharCount><pdfWordCount>6568</pdfWordCount><pdfCharCount>37451</pdfCharCount><pdfPageCount>13</pdfPageCount><abstractWordCount>87</abstractWordCount></qualityIndicators><title>Triphosgene: an efficient carbonylating agent for liquid and solid‐phase aza‐peptide synthesis. 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Application to the synthesis of two aza‐analogues of the AChR MIR decapeptide</title><title level="a" type="short" xml:lang="en">Use of triphosgene in Aza‐peptide synthesis</title><author xml:id="author-0000" role="corresp"><persName><forename type="first">Frédéric</forename><surname>André</surname></persName><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France<address><country key="FR"></country></address></affiliation><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, B.P. 451, 1 rue Grandville, 54001 Nancy, France.</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Michel</forename><surname>Marraud</surname></persName><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France<address><country key="FR"></country></address></affiliation></author><author xml:id="author-0002"><persName><forename type="first">Theodoros</forename><surname>Tsouloufis</surname></persName><affiliation>Hellenic Pasteur Institute, Athens, Greece<address><country key="GR"></country></address></affiliation></author><author xml:id="author-0003"><persName><forename type="first">Socrates J.</forename><surname>Tzartos</surname></persName><affiliation>Hellenic Pasteur Institute, Athens, Greece<address><country key="GR"></country></address></affiliation></author><author xml:id="author-0004"><persName><forename type="first">Guy</forename><surname>Boussard</surname></persName><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France<address><country key="FR"></country></address></affiliation></author><idno type="istex">8272C873EB148DD4AD01D56B5DA4DA5541D4FBAF</idno><idno type="ark">ark:/67375/WNG-9N1DS6CG-7</idno><idno type="DOI">10.1002/(SICI)1099-1387(199711)3:6<429::AID-PSC115>3.0.CO;2-C</idno><idno type="unit">PSC115</idno><idno type="toTypesetVersion">file:PSC.PSC115.pdf</idno></analytic><monogr><title level="j" type="main">Journal of Peptide Science</title><title level="j" type="alt">JOURNAL OF PEPTIDE SCIENCE</title><idno type="pISSN">1075-2617</idno><idno type="eISSN">1099-1387</idno><idno type="book-DOI">10.1002/(ISSN)1099-1387</idno><idno type="book-part-DOI">10.1002/(SICI)1099-1387(199711)3:6<>1.0.CO;2-5</idno><idno type="product">PSC</idno><imprint><biblScope unit="vol">3</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="429">429</biblScope><biblScope unit="page" to="441">441</biblScope><biblScope unit="page-count">13</biblScope><publisher>John Wiley & Sons, Ltd.</publisher><pubPlace>Chichester, UK</pubPlace><date type="published" when="1997-11"></date></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><abstract xml:lang="en" style="main"><head>Abstract</head><p>The N<hi rend="superscript">α</hi>/C<hi rend="superscript">α</hi>H exchange in aza‐peptides has the advantage of preserving the side chain. Bis(trichloromethyl)carbonate or triphosgene is a solid, stable phosgene substitute which retains its high reactivity. Temperature and coupling times are greatly reduced with reference to other usually recommended carbonylating agents, while purity and yield are increased. It has been used, in both liquid‐ and solid‐phase procedures, for the synthesis of various aza‐analogues of dipeptides, tripeptides and decapeptides containing the alanine, aspartic acid and asparagine aza‐residue. ©1997 European Peptide Society and John Wiley & Sons, Ltd.</p></abstract><textClass><keywords xml:lang="en"><term xml:id="kwd1">aza‐alanine</term><term xml:id="kwd2">aza‐asparagine</term><term xml:id="kwd3">aza‐aspartic acid</term><term xml:id="kwd4">aza‐peptides</term><term xml:id="kwd5">triphosgene</term></keywords><keywords rend="articleCategory"><term>Research Article</term></keywords><keywords rend="tocHeading1"><term>Research Articles</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/8272C873EB148DD4AD01D56B5DA4DA5541D4FBAF/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>John Wiley & Sons, Ltd.</publisherName><publisherLoc>Chichester, UK</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1099-1387</doi><issn type="print">1075-2617</issn><issn type="electronic">1099-1387</issn><idGroup><id type="product" value="PSC"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="JOURNAL OF PEPTIDE SCIENCE">Journal of Peptide Science</title><title type="subtitle">An Official Publication of the European Peptide Society</title><title type="short">J. 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Application to the synthesis of two aza‐analogues of the AChR MIR decapeptide</title><title type="short" xml:lang="en">Use of triphosgene in Aza‐peptide synthesis</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Frédéric</givenNames><familyName>André</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Michel</givenNames><familyName>Marraud</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Theodoros</givenNames><familyName>Tsouloufis</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Socrates J.</givenNames><familyName>Tzartos</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Guy</givenNames><familyName>Boussard</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="FR" type="organization"><unparsedAffiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="GR" type="organization"><unparsedAffiliation>Hellenic Pasteur Institute, Athens, Greece</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">aza‐alanine</keyword><keyword xml:id="kwd2">aza‐asparagine</keyword><keyword xml:id="kwd3">aza‐aspartic acid</keyword><keyword xml:id="kwd4">aza‐peptides</keyword><keyword xml:id="kwd5">triphosgene</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>The N<sup>α</sup>/C<sup>α</sup>H exchange in aza‐peptides has the advantage of preserving the side chain. Bis(trichloromethyl)carbonate or triphosgene is a solid, stable phosgene substitute which retains its high reactivity. Temperature and coupling times are greatly reduced with reference to other usually recommended carbonylating agents, while purity and yield are increased. It has been used, in both liquid‐ and solid‐phase procedures, for the synthesis of various aza‐analogues of dipeptides, tripeptides and decapeptides containing the alanine, aspartic acid and asparagine aza‐residue. ©1997 European Peptide Society and John Wiley & Sons, Ltd.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Triphosgene: an efficient carbonylating agent for liquid and solid‐phase aza‐peptide synthesis. Application to the synthesis of two aza‐analogues of the AChR MIR decapeptide</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Use of triphosgene in Aza‐peptide synthesis</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Triphosgene: an efficient carbonylating agent for liquid and solid‐phase aza‐peptide synthesis. Application to the synthesis of two aza‐analogues of the AChR MIR decapeptide</title></titleInfo><name type="personal"><namePart type="given">Frédéric</namePart><namePart type="family">André</namePart><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</affiliation><affiliation>Correspondence address: LCPM, CNRS‐URA‐494, ENSIC‐INPL, B.P. 451, 1 rue Grandville, 54001 Nancy, France.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Michel</namePart><namePart type="family">Marraud</namePart><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Theodoros</namePart><namePart type="family">Tsouloufis</namePart><affiliation>Hellenic Pasteur Institute, Athens, Greece</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Socrates J.</namePart><namePart type="family">Tzartos</namePart><affiliation>Hellenic Pasteur Institute, Athens, Greece</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Guy</namePart><namePart type="family">Boussard</namePart><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>John Wiley & Sons, Ltd.</publisher><place><placeTerm type="text">Chichester, UK</placeTerm></place><dateIssued encoding="w3cdtf">1997-11</dateIssued><dateCaptured encoding="w3cdtf">1996-12-12</dateCaptured><dateValid encoding="w3cdtf">1997-02-17</dateValid><copyrightDate encoding="w3cdtf">1997</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">9</extent><extent unit="tables">0</extent><extent unit="references">21</extent></physicalDescription><abstract lang="en">The Nα/CαH exchange in aza‐peptides has the advantage of preserving the side chain. Bis(trichloromethyl)carbonate or triphosgene is a solid, stable phosgene substitute which retains its high reactivity. Temperature and coupling times are greatly reduced with reference to other usually recommended carbonylating agents, while purity and yield are increased. It has been used, in both liquid‐ and solid‐phase procedures, for the synthesis of various aza‐analogues of dipeptides, tripeptides and decapeptides containing the alanine, aspartic acid and asparagine aza‐residue. ©1997 European Peptide Society and John Wiley & Sons, Ltd.</abstract><subject lang="en"><genre>keywords</genre><topic>aza‐alanine</topic><topic>aza‐asparagine</topic><topic>aza‐aspartic acid</topic><topic>aza‐peptides</topic><topic>triphosgene</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Peptide Science</title><subTitle>An Official Publication of the European Peptide Society</subTitle></titleInfo><titleInfo type="abbreviated"><title>J. 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