Susceptibility of glycans to β-elimination in Fmoc-based O-glycopeptide synthesis
order to investigate the possible extent of β‐elimination occuring in Fmoc‐based continuous‐flow solid‐phase glycopeptide synthesis, the influence of the pKb of the base used for Nα‐deprotection has been studied. A glycosylated pentapeptide as synthesized using 50%morpholine, 10%, piperidine or 2% D...
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| Veröffentlicht in: | International Journal of Peptide and Protein Research 1994-06, Vol.43 (6), p.529-536 |
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| container_title | International Journal of Peptide and Protein Research |
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| creator | MELDAL, MORTEN BIELFELDT, TIM PETERS, STEFAN JENSEN, KNUD J. PAULSEN, HANS BOCK, KLAUS |
| description | order to investigate the possible extent of β‐elimination occuring in Fmoc‐based continuous‐flow solid‐phase glycopeptide synthesis, the influence of the pKb of the base used for Nα‐deprotection has been studied. A glycosylated pentapeptide as synthesized using 50%morpholine, 10%, piperidine or 2% DBU, respectively, in DMF for deprotection. The dehydropentapeptide Nα‐.Ac‐Thr‐Thr‐δAba‐Val‐Thr‐NH2, which would be formed in the case of β‐elimination, was prepared independently and used as a control in HPLC analysis; however, this product was not formed under any of the deprotection conditions applied. Furthermore, a 23 amino acid long glycopeptide from human intestinal mucin was prepared using 2% DBU as a base for Fmoc cleavage, and similarly no β‐elimination was observed. The glycopeptide products were subjected to a prolonged treatment with sodium hydroxide in methanol/water without significant formation of byproducts, and the pure glycopeptides were isolated and characterized by 1H‐NMR spectroscopy. |
| doi_str_mv | 10.1111/j.1399-3011.1994.tb00554.x |
| format | Article |
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A glycosylated pentapeptide as synthesized using 50%morpholine, 10%, piperidine or 2% DBU, respectively, in DMF for deprotection. The dehydropentapeptide Nα‐.Ac‐Thr‐Thr‐δAba‐Val‐Thr‐NH2, which would be formed in the case of β‐elimination, was prepared independently and used as a control in HPLC analysis; however, this product was not formed under any of the deprotection conditions applied. Furthermore, a 23 amino acid long glycopeptide from human intestinal mucin was prepared using 2% DBU as a base for Fmoc cleavage, and similarly no β‐elimination was observed. 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A glycosylated pentapeptide as synthesized using 50%morpholine, 10%, piperidine or 2% DBU, respectively, in DMF for deprotection. The dehydropentapeptide Nα‐.Ac‐Thr‐Thr‐δAba‐Val‐Thr‐NH2, which would be formed in the case of β‐elimination, was prepared independently and used as a control in HPLC analysis; however, this product was not formed under any of the deprotection conditions applied. Furthermore, a 23 amino acid long glycopeptide from human intestinal mucin was prepared using 2% DBU as a base for Fmoc cleavage, and similarly no β‐elimination was observed. The glycopeptide products were subjected to a prolonged treatment with sodium hydroxide in methanol/water without significant formation of byproducts, and the pure glycopeptides were isolated and characterized by 1H‐NMR spectroscopy.</description><subject>Amino Acid Sequence</subject><subject>Amino Acids - chemistry</subject><subject>azide reduction</subject><subject>Bridged Bicyclo Compounds</subject><subject>Chemistry</subject><subject>dehydropeptide</subject><subject>Exact sciences and technology</subject><subject>Fluorenes - chemistry</subject><subject>Fmoc cleavage</subject><subject>Glycopeptides - chemical synthesis</subject><subject>human intestinal mucin</subject><subject>Molecular Sequence Data</subject><subject>much glycopeptide</subject><subject>Mucins - chemical synthesis</subject><subject>N-acetyl-α-D-galactopyranose</subject><subject>O-linked glycopeptide</subject><subject>Organic chemistry</subject><subject>Peptides</subject><subject>Polysaccharides - chemistry</subject><subject>Preparations and properties</subject><subject>solid-phase glycopeptide synthesis</subject><subject>β-elimination</subject><issn>0367-8377</issn><issn>1399-3011</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkM1O3DAUha0KBAPtIyBFCLFzsGMnjtmgMjBMpVGRWqouLce5bj3kZxpnxOS1eJA-Ux1NNPt6cxf3nONzP4QuKYlpeDfrmDIpMSOUxlRKHvcFIWnK490HNDusjtCMsEzgnAlxis68XxPCOBPJCToRMslJzmbo2_etN7DpXeEq1w9Ra6Nf1WB046O-jf6-Y6hc7Rrdu7aJXBMt6tbgQnsoo2c8KtvN6C4h8kPT_wbv_Ed0bHXl4dM0z9GPxePLfIlXz09f5p9X2IQSEpclJSWnBUtoaEUhtZBLXQiWsFKKnAIYnVAjqNCptbkBRrIss1JQwkWRWXaOrve5m679swXfq9qFW6pKN9BuvRKZ4AlJZRDe7oWma73vwKpN52rdDYoSNQJVazVSUyM1NQJVE1C1C-aL6ZdtUUN5sE4Ew_5q2mtvdGU73RjnDzJOc5knPMju9rI3V8HwHwXU_P7hIU3GK_A-wfkedocE3b2qTDCRqp9fn9Ry_hLGiivC_gH4oqLJ</recordid><startdate>199406</startdate><enddate>199406</enddate><creator>MELDAL, MORTEN</creator><creator>BIELFELDT, TIM</creator><creator>PETERS, STEFAN</creator><creator>JENSEN, KNUD J.</creator><creator>PAULSEN, HANS</creator><creator>BOCK, KLAUS</creator><general>Blackwell Publishing Ltd</general><general>Munksgaard</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>199406</creationdate><title>Susceptibility of glycans to β-elimination in Fmoc-based O-glycopeptide synthesis</title><author>MELDAL, MORTEN ; BIELFELDT, TIM ; PETERS, STEFAN ; JENSEN, KNUD J. ; PAULSEN, HANS ; BOCK, KLAUS</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4379-dd10d41b3213431e5fe89ab7323d9781eeca21c717a5ff8ce30666f971047b6f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acids - chemistry</topic><topic>azide reduction</topic><topic>Bridged Bicyclo Compounds</topic><topic>Chemistry</topic><topic>dehydropeptide</topic><topic>Exact sciences and technology</topic><topic>Fluorenes - chemistry</topic><topic>Fmoc cleavage</topic><topic>Glycopeptides - chemical synthesis</topic><topic>human intestinal mucin</topic><topic>Molecular Sequence Data</topic><topic>much glycopeptide</topic><topic>Mucins - chemical synthesis</topic><topic>N-acetyl-α-D-galactopyranose</topic><topic>O-linked glycopeptide</topic><topic>Organic chemistry</topic><topic>Peptides</topic><topic>Polysaccharides - chemistry</topic><topic>Preparations and properties</topic><topic>solid-phase glycopeptide synthesis</topic><topic>β-elimination</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MELDAL, MORTEN</creatorcontrib><creatorcontrib>BIELFELDT, TIM</creatorcontrib><creatorcontrib>PETERS, STEFAN</creatorcontrib><creatorcontrib>JENSEN, KNUD J.</creatorcontrib><creatorcontrib>PAULSEN, HANS</creatorcontrib><creatorcontrib>BOCK, KLAUS</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>International Journal of Peptide and Protein Research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MELDAL, MORTEN</au><au>BIELFELDT, TIM</au><au>PETERS, STEFAN</au><au>JENSEN, KNUD J.</au><au>PAULSEN, HANS</au><au>BOCK, KLAUS</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Susceptibility of glycans to β-elimination in Fmoc-based O-glycopeptide synthesis</atitle><jtitle>International Journal of Peptide and Protein Research</jtitle><addtitle>Int J Pept Protein Res</addtitle><date>1994-06</date><risdate>1994</risdate><volume>43</volume><issue>6</issue><spage>529</spage><epage>536</epage><pages>529-536</pages><issn>0367-8377</issn><eissn>1399-3011</eissn><coden>IJPPC3</coden><abstract>order to investigate the possible extent of β‐elimination occuring in Fmoc‐based continuous‐flow solid‐phase glycopeptide synthesis, the influence of the pKb of the base used for Nα‐deprotection has been studied. A glycosylated pentapeptide as synthesized using 50%morpholine, 10%, piperidine or 2% DBU, respectively, in DMF for deprotection. The dehydropentapeptide Nα‐.Ac‐Thr‐Thr‐δAba‐Val‐Thr‐NH2, which would be formed in the case of β‐elimination, was prepared independently and used as a control in HPLC analysis; however, this product was not formed under any of the deprotection conditions applied. Furthermore, a 23 amino acid long glycopeptide from human intestinal mucin was prepared using 2% DBU as a base for Fmoc cleavage, and similarly no β‐elimination was observed. The glycopeptide products were subjected to a prolonged treatment with sodium hydroxide in methanol/water without significant formation of byproducts, and the pure glycopeptides were isolated and characterized by 1H‐NMR spectroscopy.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>7928083</pmid><doi>10.1111/j.1399-3011.1994.tb00554.x</doi><tpages>8</tpages></addata></record> |
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| ispartof | International Journal of Peptide and Protein Research, 1994-06, Vol.43 (6), p.529-536 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Amino Acid Sequence Amino Acids - chemistry azide reduction Bridged Bicyclo Compounds Chemistry dehydropeptide Exact sciences and technology Fluorenes - chemistry Fmoc cleavage Glycopeptides - chemical synthesis human intestinal mucin Molecular Sequence Data much glycopeptide Mucins - chemical synthesis N-acetyl-α-D-galactopyranose O-linked glycopeptide Organic chemistry Peptides Polysaccharides - chemistry Preparations and properties solid-phase glycopeptide synthesis β-elimination |
| title | Susceptibility of glycans to β-elimination in Fmoc-based O-glycopeptide synthesis |
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