Loading…

Chemoenzymatic synthesis of para-nitrophenol (pNP)-tagged alpha 2-8-sialosides and high-throughput substrate specificity studies of alpha 2-8-sialidases

para-Nitrophenol (pNP)-tagged alpha 2-8-linked sialosides containing different sialic acid forms were chemoenzymatically synthesized using an efficient one-pot three-enzyme alpha 2-8-sialylation system. The resulting compounds allowed high-throughput substrate specificity studies of the alpha 2-8-si...

Full description

Saved in:
Bibliographic Details
Published in:Organic & biomolecular chemistry 2017-01, Vol.15 (1), p.160-167
Main Authors: Tasnima, Nova, Yu, Hai, Li, Yanhong, Santra, Abhishek, Chen, Xi
Format: Article
Language:English
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page 167
container_issue 1
container_start_page 160
container_title Organic & biomolecular chemistry
container_volume 15
creator Tasnima, Nova
Yu, Hai
Li, Yanhong
Santra, Abhishek
Chen, Xi
description para-Nitrophenol (pNP)-tagged alpha 2-8-linked sialosides containing different sialic acid forms were chemoenzymatically synthesized using an efficient one-pot three-enzyme alpha 2-8-sialylation system. The resulting compounds allowed high-throughput substrate specificity studies of the alpha 2-8-sialidase activity of a recombinant human cytosolic sialidase hNEU2 and various bacterial sialidases. The sialoside substrate profiles obtained can be used to guide the selection of suitable sialidases for sialylglycan analysis and for cell and tissue surface glycan modification. They can also be used to guide sialidase inhibitor design.
doi_str_mv 10.1039/c6ob02240e
format article
fullrecord <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_miscellaneous_1859488548</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1859488548</sourcerecordid><originalsourceid>FETCH-LOGICAL-p118t-e08b477b4fc0ce1b2148912cb86592f97935d658145a469bd3899654afe890323</originalsourceid><addsrcrecordid>eNpVj71OwzAURi0EEqWw8AQey2CwHTuxR1TxJyFggLlynJvEKI1NrjOUJ-FxQYCQmM43nU-HkFPBzwUv7IUvY82lVBz2yEKoqmJcF3b_b0t-SI4QXzkXtirVgnyse9hGGN93W5eDp7gbcw8YkMaWJjc5NoY8xdTDGAe6Sg9PZyy7roOGuiH1jkpmGAY3RAwNIHVjQ_vQ9Sz3U5y7Ps2Z4lxjnlwGigl8aIMPeUcxz02A75__ptA4BDwmB60bEE5-uSQv11fP61t2_3hzt768Z0kIkxlwU3-l1ar13IOopVDGCulrU2orW1vZQjelNkJpp0pbN4WxttTKtWAsL2SxJKsfb5ri2wyYN9uAHobBjRBn3AijrTJGK1N8AkCBbFk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1859488548</pqid></control><display><type>article</type><title>Chemoenzymatic synthesis of para-nitrophenol (pNP)-tagged alpha 2-8-sialosides and high-throughput substrate specificity studies of alpha 2-8-sialidases</title><source>Royal Society of Chemistry:Jisc Collections:Royal Society of Chemistry Read and Publish 2022-2024 (reading list)</source><creator>Tasnima, Nova ; Yu, Hai ; Li, Yanhong ; Santra, Abhishek ; Chen, Xi</creator><creatorcontrib>Tasnima, Nova ; Yu, Hai ; Li, Yanhong ; Santra, Abhishek ; Chen, Xi</creatorcontrib><description>para-Nitrophenol (pNP)-tagged alpha 2-8-linked sialosides containing different sialic acid forms were chemoenzymatically synthesized using an efficient one-pot three-enzyme alpha 2-8-sialylation system. The resulting compounds allowed high-throughput substrate specificity studies of the alpha 2-8-sialidase activity of a recombinant human cytosolic sialidase hNEU2 and various bacterial sialidases. The sialoside substrate profiles obtained can be used to guide the selection of suitable sialidases for sialylglycan analysis and for cell and tissue surface glycan modification. They can also be used to guide sialidase inhibitor design.</description><identifier>ISSN: 1477-0520</identifier><identifier>EISSN: 1477-0539</identifier><identifier>DOI: 10.1039/c6ob02240e</identifier><language>eng</language><ispartof>Organic &amp; biomolecular chemistry, 2017-01, Vol.15 (1), p.160-167</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></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></links><search><creatorcontrib>Tasnima, Nova</creatorcontrib><creatorcontrib>Yu, Hai</creatorcontrib><creatorcontrib>Li, Yanhong</creatorcontrib><creatorcontrib>Santra, Abhishek</creatorcontrib><creatorcontrib>Chen, Xi</creatorcontrib><title>Chemoenzymatic synthesis of para-nitrophenol (pNP)-tagged alpha 2-8-sialosides and high-throughput substrate specificity studies of alpha 2-8-sialidases</title><title>Organic &amp; biomolecular chemistry</title><description>para-Nitrophenol (pNP)-tagged alpha 2-8-linked sialosides containing different sialic acid forms were chemoenzymatically synthesized using an efficient one-pot three-enzyme alpha 2-8-sialylation system. The resulting compounds allowed high-throughput substrate specificity studies of the alpha 2-8-sialidase activity of a recombinant human cytosolic sialidase hNEU2 and various bacterial sialidases. The sialoside substrate profiles obtained can be used to guide the selection of suitable sialidases for sialylglycan analysis and for cell and tissue surface glycan modification. They can also be used to guide sialidase inhibitor design.</description><issn>1477-0520</issn><issn>1477-0539</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNpVj71OwzAURi0EEqWw8AQey2CwHTuxR1TxJyFggLlynJvEKI1NrjOUJ-FxQYCQmM43nU-HkFPBzwUv7IUvY82lVBz2yEKoqmJcF3b_b0t-SI4QXzkXtirVgnyse9hGGN93W5eDp7gbcw8YkMaWJjc5NoY8xdTDGAe6Sg9PZyy7roOGuiH1jkpmGAY3RAwNIHVjQ_vQ9Sz3U5y7Ps2Z4lxjnlwGigl8aIMPeUcxz02A75__ptA4BDwmB60bEE5-uSQv11fP61t2_3hzt768Z0kIkxlwU3-l1ar13IOopVDGCulrU2orW1vZQjelNkJpp0pbN4WxttTKtWAsL2SxJKsfb5ri2wyYN9uAHobBjRBn3AijrTJGK1N8AkCBbFk</recordid><startdate>20170107</startdate><enddate>20170107</enddate><creator>Tasnima, Nova</creator><creator>Yu, Hai</creator><creator>Li, Yanhong</creator><creator>Santra, Abhishek</creator><creator>Chen, Xi</creator><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20170107</creationdate><title>Chemoenzymatic synthesis of para-nitrophenol (pNP)-tagged alpha 2-8-sialosides and high-throughput substrate specificity studies of alpha 2-8-sialidases</title><author>Tasnima, Nova ; Yu, Hai ; Li, Yanhong ; Santra, Abhishek ; Chen, Xi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p118t-e08b477b4fc0ce1b2148912cb86592f97935d658145a469bd3899654afe890323</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tasnima, Nova</creatorcontrib><creatorcontrib>Yu, Hai</creatorcontrib><creatorcontrib>Li, Yanhong</creatorcontrib><creatorcontrib>Santra, Abhishek</creatorcontrib><creatorcontrib>Chen, Xi</creatorcontrib><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Organic &amp; biomolecular chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tasnima, Nova</au><au>Yu, Hai</au><au>Li, Yanhong</au><au>Santra, Abhishek</au><au>Chen, Xi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chemoenzymatic synthesis of para-nitrophenol (pNP)-tagged alpha 2-8-sialosides and high-throughput substrate specificity studies of alpha 2-8-sialidases</atitle><jtitle>Organic &amp; biomolecular chemistry</jtitle><date>2017-01-07</date><risdate>2017</risdate><volume>15</volume><issue>1</issue><spage>160</spage><epage>167</epage><pages>160-167</pages><issn>1477-0520</issn><eissn>1477-0539</eissn><abstract>para-Nitrophenol (pNP)-tagged alpha 2-8-linked sialosides containing different sialic acid forms were chemoenzymatically synthesized using an efficient one-pot three-enzyme alpha 2-8-sialylation system. The resulting compounds allowed high-throughput substrate specificity studies of the alpha 2-8-sialidase activity of a recombinant human cytosolic sialidase hNEU2 and various bacterial sialidases. The sialoside substrate profiles obtained can be used to guide the selection of suitable sialidases for sialylglycan analysis and for cell and tissue surface glycan modification. They can also be used to guide sialidase inhibitor design.</abstract><doi>10.1039/c6ob02240e</doi><tpages>8</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1477-0520
ispartof Organic & biomolecular chemistry, 2017-01, Vol.15 (1), p.160-167
issn 1477-0520
1477-0539
language eng
recordid cdi_proquest_miscellaneous_1859488548
source Royal Society of Chemistry:Jisc Collections:Royal Society of Chemistry Read and Publish 2022-2024 (reading list)
title Chemoenzymatic synthesis of para-nitrophenol (pNP)-tagged alpha 2-8-sialosides and high-throughput substrate specificity studies of alpha 2-8-sialidases
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T13%3A02%3A49IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Chemoenzymatic%20synthesis%20of%20para-nitrophenol%20(pNP)-tagged%20alpha%202-8-sialosides%20and%20high-throughput%20substrate%20specificity%20studies%20of%20alpha%202-8-sialidases&rft.jtitle=Organic%20&%20biomolecular%20chemistry&rft.au=Tasnima,%20Nova&rft.date=2017-01-07&rft.volume=15&rft.issue=1&rft.spage=160&rft.epage=167&rft.pages=160-167&rft.issn=1477-0520&rft.eissn=1477-0539&rft_id=info:doi/10.1039/c6ob02240e&rft_dat=%3Cproquest%3E1859488548%3C/proquest%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-p118t-e08b477b4fc0ce1b2148912cb86592f97935d658145a469bd3899654afe890323%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1859488548&rft_id=info:pmid/&rfr_iscdi=true