Synthesis and enzymatic susceptibility of a series of novel GM2 analogs
A series of GM2 analogs in which GM2 epitope was coupled to a variety of glycosyl lipids were designed and synthesized to investigate the mechanism of enzymatic hydrolysis of GM2 ganglioside. The coupling of N-Troc-protected sialic acid and p-methoxyphenyl galactoside acceptor gave the crystalline d...
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| Veröffentlicht in: | Glycoconjugate journal 2006-07, Vol.23 (5-6), p.329-343 |
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| container_end_page | 343 |
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| container_issue | 5-6 |
| container_start_page | 329 |
| container_title | Glycoconjugate journal |
| container_volume | 23 |
| creator | Fuse, Tomoaki Ando, Hiromune Imamura, Akihiro Sawada, Naoki Ishida, Hideharu Kiso, Makoto Ando, Takayuki Li, Su-Chen Li, Yu-Teh |
| description | A series of GM2 analogs in which GM2 epitope was coupled to a variety of glycosyl lipids were designed and synthesized to investigate the mechanism of enzymatic hydrolysis of GM2 ganglioside. The coupling of N-Troc-protected sialic acid and p-methoxyphenyl galactoside acceptor gave the crystalline disaccharide, which was further coupled with galactosamine donor to give the desired GM2 epitope trisaccharide. After conversion into the corresponding glycosyl donor, the trisaccharide was coupled with galactose, glucose and artificial ceramide (B30) to give the final compounds. The result on hydrolysis of GM2 analogs indicates that GM2 activator protein requires one spacer sugar between GM2 epitope and the lipid moiety to assist the hydrolysis of the terminal GalNAc residue. |
| doi_str_mv | 10.1007/s10719-006-5704-9 |
| format | Article |
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The coupling of N-Troc-protected sialic acid and p-methoxyphenyl galactoside acceptor gave the crystalline disaccharide, which was further coupled with galactosamine donor to give the desired GM2 epitope trisaccharide. After conversion into the corresponding glycosyl donor, the trisaccharide was coupled with galactose, glucose and artificial ceramide (B30) to give the final compounds. The result on hydrolysis of GM2 analogs indicates that GM2 activator protein requires one spacer sugar between GM2 epitope and the lipid moiety to assist the hydrolysis of the terminal GalNAc residue.</description><identifier>ISSN: 0282-0080</identifier><identifier>EISSN: 1573-4986</identifier><identifier>DOI: 10.1007/s10719-006-5704-9</identifier><identifier>PMID: 16897176</identifier><language>eng</language><publisher>United States: Springer Nature B.V</publisher><subject>Enzymes - chemistry ; Enzymes - metabolism ; Enzymes - physiology ; Epitopes - chemistry ; Epitopes - metabolism ; G(M2) Ganglioside - analogs & derivatives ; G(M2) Ganglioside - chemical synthesis ; G(M2) Ganglioside - chemistry ; G(M2) Ganglioside - metabolism ; Humans ; Hydrolysis ; Proteins ; Tay-Sachs Disease - enzymology ; Tay-Sachs Disease - metabolism</subject><ispartof>Glycoconjugate journal, 2006-07, Vol.23 (5-6), p.329-343</ispartof><rights>Springer Science + Business Media, LLC 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c462t-240d946e420fc5bd203109fd6c216b9146fcb6241f7f1fef9155fb174674897b3</citedby><cites>FETCH-LOGICAL-c462t-240d946e420fc5bd203109fd6c216b9146fcb6241f7f1fef9155fb174674897b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16897176$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fuse, Tomoaki</creatorcontrib><creatorcontrib>Ando, Hiromune</creatorcontrib><creatorcontrib>Imamura, Akihiro</creatorcontrib><creatorcontrib>Sawada, Naoki</creatorcontrib><creatorcontrib>Ishida, Hideharu</creatorcontrib><creatorcontrib>Kiso, Makoto</creatorcontrib><creatorcontrib>Ando, Takayuki</creatorcontrib><creatorcontrib>Li, Su-Chen</creatorcontrib><creatorcontrib>Li, Yu-Teh</creatorcontrib><title>Synthesis and enzymatic susceptibility of a series of novel GM2 analogs</title><title>Glycoconjugate journal</title><addtitle>Glycoconj J</addtitle><description>A series of GM2 analogs in which GM2 epitope was coupled to a variety of glycosyl lipids were designed and synthesized to investigate the mechanism of enzymatic hydrolysis of GM2 ganglioside. 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The result on hydrolysis of GM2 analogs indicates that GM2 activator protein requires one spacer sugar between GM2 epitope and the lipid moiety to assist the hydrolysis of the terminal GalNAc residue.</description><subject>Enzymes - chemistry</subject><subject>Enzymes - metabolism</subject><subject>Enzymes - physiology</subject><subject>Epitopes - chemistry</subject><subject>Epitopes - metabolism</subject><subject>G(M2) Ganglioside - analogs & derivatives</subject><subject>G(M2) Ganglioside - chemical synthesis</subject><subject>G(M2) Ganglioside - chemistry</subject><subject>G(M2) Ganglioside - metabolism</subject><subject>Humans</subject><subject>Hydrolysis</subject><subject>Proteins</subject><subject>Tay-Sachs Disease - enzymology</subject><subject>Tay-Sachs Disease - metabolism</subject><issn>0282-0080</issn><issn>1573-4986</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpdkEtLxDAUhYMozjj6A9xIceGuem-a5rEU0VEYcaGuQx-Jduhj7G2F-uvNMAOCq1zIdw6Hj7FzhGsEUDeEoNDEADJOFYjYHLA5piqJhdHykM2Bax5-NczYCdEaQkZwfcxmKLVRqOScLV-ndvh0VFGUtWXk2p-pyYaqiGikwm2GKq_qapiizkdZRK6vHG3vtvt2dbR85iGV1d0HnbIjn9Xkzvbvgr0_3L_dPcarl-XT3e0qLoTkQ8wFlEZIJzj4Is1LDgmC8aUsOMrcoJC-yCUX6JVH77zBNPU5KiGVCJPzZMGudr2bvvsaHQ22qcLQus5a141kpVZcgTIBvPwHrruxD2PJqlSLlOtEBAh3UNF3RL3zdtNXTdZPFsFuFdudYhsU261iuy2-2BePeePKv8TeafIL52h1Yg</recordid><startdate>20060701</startdate><enddate>20060701</enddate><creator>Fuse, Tomoaki</creator><creator>Ando, Hiromune</creator><creator>Imamura, Akihiro</creator><creator>Sawada, Naoki</creator><creator>Ishida, Hideharu</creator><creator>Kiso, Makoto</creator><creator>Ando, Takayuki</creator><creator>Li, Su-Chen</creator><creator>Li, Yu-Teh</creator><general>Springer Nature B.V</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>3V.</scope><scope>7T5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20060701</creationdate><title>Synthesis and enzymatic susceptibility of a series of novel GM2 analogs</title><author>Fuse, Tomoaki ; 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| subjects | Enzymes - chemistry Enzymes - metabolism Enzymes - physiology Epitopes - chemistry Epitopes - metabolism G(M2) Ganglioside - analogs & derivatives G(M2) Ganglioside - chemical synthesis G(M2) Ganglioside - chemistry G(M2) Ganglioside - metabolism Humans Hydrolysis Proteins Tay-Sachs Disease - enzymology Tay-Sachs Disease - metabolism |
| title | Synthesis and enzymatic susceptibility of a series of novel GM2 analogs |
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