Effects of glycosylation on fragments of tumour associated human epithelial mucin MUC1
The glycodecapeptide AcPAPGS(alpha GalNAc)T(alpha GalNAc)APPA and the C-terminal glycohexapeptide AcS(alpha GalNAc)T(alpha GalNAc)APPA have been synthesized by applying the N-terminal Fmoc group in combination with the heptyl ester cleavable by lipase-catalyzed hydrolysis at pH 7. The solution confo...
Gespeichert in:
| Veröffentlicht in: | Bioorganic & medicinal chemistry 1998-09, Vol.6 (9), p.1531-1545 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1545 |
|---|---|
| container_issue | 9 |
| container_start_page | 1531 |
| container_title | Bioorganic & medicinal chemistry |
| container_volume | 6 |
| creator | Braun, P Davies, G M Price, M R Williams, P M Tendler, S J Kunz, H |
| description | The glycodecapeptide AcPAPGS(alpha GalNAc)T(alpha GalNAc)APPA and the C-terminal glycohexapeptide AcS(alpha GalNAc)T(alpha GalNAc)APPA have been synthesized by applying the N-terminal Fmoc group in combination with the heptyl ester cleavable by lipase-catalyzed hydrolysis at pH 7. The solution conformation of these MUC1-related synthetic glycopeptides and the control, non-glycosylated decapeptide AcPAPGSTAPPA have been investigated using NMR spectroscopy. The structural studies indicate that the glycohexapeptide has a folded structure in solution. For this molecule, unrestrained molecular dynamics has been used to confirm the presence of the observed solution through-space connections. The results indicate that the non-globular nature of MUC1 is due to both protein core sequence and the effect of carbohydrate. |
| doi_str_mv | 10.1016/S0968-0896(98)00092-3 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_70020845</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>70020845</sourcerecordid><originalsourceid>FETCH-LOGICAL-c304t-8ee2888eecad6a4dac58b25bd5e8fe1cae94f0013f82aa5359257a2c89a8621b3</originalsourceid><addsrcrecordid>eNo9kMFOwzAMhnMAjTF4hEk5ITgUkrTpkiOaNkAa4gDjGrmpsxW1zWjSw96ejk2TLP-S7d-WP0KmnD1yxvOnT6ZzlTCl83utHhhjWiTpBRmfy1fkOoSfoSEyzUdkpBXjSsgx-V44hzYG6h3d1Hvrw76GWPmWDuE62DTYHruxb3zfUQjB2woilnTbN9BS3FVxi3UFNW16W7X0fT3nN-TSQR3w9qQTsl4uvuavyerj5W3-vEpsyrKYKESh1JAtlDlkJVipCiGLUqJyyC2gzhxjPHVKAMhUaiFnIKzSoHLBi3RC7o57d53_7TFE01TBYl1Di74PZjZ8zFQmh0F5HLSdD6FDZ3Zd1UC3N5yZA0Pzz9AcYBk96IGhSQff9HSgLxosz64TwPQPcilwQg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>70020845</pqid></control><display><type>article</type><title>Effects of glycosylation on fragments of tumour associated human epithelial mucin MUC1</title><source>Elsevier ScienceDirect Journals Complete - AutoHoldings</source><source>MEDLINE</source><creator>Braun, P ; Davies, G M ; Price, M R ; Williams, P M ; Tendler, S J ; Kunz, H</creator><creatorcontrib>Braun, P ; Davies, G M ; Price, M R ; Williams, P M ; Tendler, S J ; Kunz, H</creatorcontrib><description>The glycodecapeptide AcPAPGS(alpha GalNAc)T(alpha GalNAc)APPA and the C-terminal glycohexapeptide AcS(alpha GalNAc)T(alpha GalNAc)APPA have been synthesized by applying the N-terminal Fmoc group in combination with the heptyl ester cleavable by lipase-catalyzed hydrolysis at pH 7. The solution conformation of these MUC1-related synthetic glycopeptides and the control, non-glycosylated decapeptide AcPAPGSTAPPA have been investigated using NMR spectroscopy. The structural studies indicate that the glycohexapeptide has a folded structure in solution. For this molecule, unrestrained molecular dynamics has been used to confirm the presence of the observed solution through-space connections. The results indicate that the non-globular nature of MUC1 is due to both protein core sequence and the effect of carbohydrate.</description><identifier>ISSN: 0968-0896</identifier><identifier>DOI: 10.1016/S0968-0896(98)00092-3</identifier><identifier>PMID: 9801825</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Glycosylation ; Humans ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Mucin-1 - chemistry ; Mucin-1 - metabolism ; Peptide Fragments - metabolism ; Protein Conformation ; Spectrometry, Mass, Fast Atom Bombardment</subject><ispartof>Bioorganic & medicinal chemistry, 1998-09, Vol.6 (9), p.1531-1545</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c304t-8ee2888eecad6a4dac58b25bd5e8fe1cae94f0013f82aa5359257a2c89a8621b3</citedby><cites>FETCH-LOGICAL-c304t-8ee2888eecad6a4dac58b25bd5e8fe1cae94f0013f82aa5359257a2c89a8621b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27907,27908</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9801825$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Braun, P</creatorcontrib><creatorcontrib>Davies, G M</creatorcontrib><creatorcontrib>Price, M R</creatorcontrib><creatorcontrib>Williams, P M</creatorcontrib><creatorcontrib>Tendler, S J</creatorcontrib><creatorcontrib>Kunz, H</creatorcontrib><title>Effects of glycosylation on fragments of tumour associated human epithelial mucin MUC1</title><title>Bioorganic & medicinal chemistry</title><addtitle>Bioorg Med Chem</addtitle><description>The glycodecapeptide AcPAPGS(alpha GalNAc)T(alpha GalNAc)APPA and the C-terminal glycohexapeptide AcS(alpha GalNAc)T(alpha GalNAc)APPA have been synthesized by applying the N-terminal Fmoc group in combination with the heptyl ester cleavable by lipase-catalyzed hydrolysis at pH 7. The solution conformation of these MUC1-related synthetic glycopeptides and the control, non-glycosylated decapeptide AcPAPGSTAPPA have been investigated using NMR spectroscopy. The structural studies indicate that the glycohexapeptide has a folded structure in solution. For this molecule, unrestrained molecular dynamics has been used to confirm the presence of the observed solution through-space connections. The results indicate that the non-globular nature of MUC1 is due to both protein core sequence and the effect of carbohydrate.</description><subject>Amino Acid Sequence</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mucin-1 - chemistry</subject><subject>Mucin-1 - metabolism</subject><subject>Peptide Fragments - metabolism</subject><subject>Protein Conformation</subject><subject>Spectrometry, Mass, Fast Atom Bombardment</subject><issn>0968-0896</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMFOwzAMhnMAjTF4hEk5ITgUkrTpkiOaNkAa4gDjGrmpsxW1zWjSw96ejk2TLP-S7d-WP0KmnD1yxvOnT6ZzlTCl83utHhhjWiTpBRmfy1fkOoSfoSEyzUdkpBXjSsgx-V44hzYG6h3d1Hvrw76GWPmWDuE62DTYHruxb3zfUQjB2woilnTbN9BS3FVxi3UFNW16W7X0fT3nN-TSQR3w9qQTsl4uvuavyerj5W3-vEpsyrKYKESh1JAtlDlkJVipCiGLUqJyyC2gzhxjPHVKAMhUaiFnIKzSoHLBi3RC7o57d53_7TFE01TBYl1Di74PZjZ8zFQmh0F5HLSdD6FDZ3Zd1UC3N5yZA0Pzz9AcYBk96IGhSQff9HSgLxosz64TwPQPcilwQg</recordid><startdate>199809</startdate><enddate>199809</enddate><creator>Braun, P</creator><creator>Davies, G M</creator><creator>Price, M R</creator><creator>Williams, P M</creator><creator>Tendler, S J</creator><creator>Kunz, H</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></search><sort><creationdate>199809</creationdate><title>Effects of glycosylation on fragments of tumour associated human epithelial mucin MUC1</title><author>Braun, P ; Davies, G M ; Price, M R ; Williams, P M ; Tendler, S J ; Kunz, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c304t-8ee2888eecad6a4dac58b25bd5e8fe1cae94f0013f82aa5359257a2c89a8621b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mucin-1 - chemistry</topic><topic>Mucin-1 - metabolism</topic><topic>Peptide Fragments - metabolism</topic><topic>Protein Conformation</topic><topic>Spectrometry, Mass, Fast Atom Bombardment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Braun, P</creatorcontrib><creatorcontrib>Davies, G M</creatorcontrib><creatorcontrib>Price, M R</creatorcontrib><creatorcontrib>Williams, P M</creatorcontrib><creatorcontrib>Tendler, S J</creatorcontrib><creatorcontrib>Kunz, H</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>Bioorganic & medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Braun, P</au><au>Davies, G M</au><au>Price, M R</au><au>Williams, P M</au><au>Tendler, S J</au><au>Kunz, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of glycosylation on fragments of tumour associated human epithelial mucin MUC1</atitle><jtitle>Bioorganic & medicinal chemistry</jtitle><addtitle>Bioorg Med Chem</addtitle><date>1998-09</date><risdate>1998</risdate><volume>6</volume><issue>9</issue><spage>1531</spage><epage>1545</epage><pages>1531-1545</pages><issn>0968-0896</issn><abstract>The glycodecapeptide AcPAPGS(alpha GalNAc)T(alpha GalNAc)APPA and the C-terminal glycohexapeptide AcS(alpha GalNAc)T(alpha GalNAc)APPA have been synthesized by applying the N-terminal Fmoc group in combination with the heptyl ester cleavable by lipase-catalyzed hydrolysis at pH 7. The solution conformation of these MUC1-related synthetic glycopeptides and the control, non-glycosylated decapeptide AcPAPGSTAPPA have been investigated using NMR spectroscopy. The structural studies indicate that the glycohexapeptide has a folded structure in solution. For this molecule, unrestrained molecular dynamics has been used to confirm the presence of the observed solution through-space connections. The results indicate that the non-globular nature of MUC1 is due to both protein core sequence and the effect of carbohydrate.</abstract><cop>England</cop><pmid>9801825</pmid><doi>10.1016/S0968-0896(98)00092-3</doi><tpages>15</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0968-0896 |
| ispartof | Bioorganic & medicinal chemistry, 1998-09, Vol.6 (9), p.1531-1545 |
| issn | 0968-0896 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70020845 |
| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE |
| subjects | Amino Acid Sequence Glycosylation Humans Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Mucin-1 - chemistry Mucin-1 - metabolism Peptide Fragments - metabolism Protein Conformation Spectrometry, Mass, Fast Atom Bombardment |
| title | Effects of glycosylation on fragments of tumour associated human epithelial mucin MUC1 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-16T11%3A06%3A40IST&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=Effects%20of%20glycosylation%20on%20fragments%20of%20tumour%20associated%20human%20epithelial%20mucin%20MUC1&rft.jtitle=Bioorganic%20&%20medicinal%20chemistry&rft.au=Braun,%20P&rft.date=1998-09&rft.volume=6&rft.issue=9&rft.spage=1531&rft.epage=1545&rft.pages=1531-1545&rft.issn=0968-0896&rft_id=info:doi/10.1016/S0968-0896(98)00092-3&rft_dat=%3Cproquest_cross%3E70020845%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=70020845&rft_id=info:pmid/9801825&rfr_iscdi=true |