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Systematic chemoenzymatic synthesis of O-sulfated sialyl Lewis x antigens
O-Sulfated sialyl Lewis x antigens play important roles in nature. However, due to their structural complexity, they are not readily accessible by either chemical or enzymatic synthetic processes. Taking advantage of a bacterial sialyltransferase mutant that can catalyze the transfer of different si...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Royal Society of Chemistry
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5269574/ https://www.ncbi.nlm.nih.gov/pubmed/28138383 http://dx.doi.org/10.1039/c5sc04104j |
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author | Santra, Abhishek Yu, Hai Tasnima, Nova Muthana, Musleh M. Li, Yanhong Zeng, Jie Kenyon, Nicholas J. Louie, Angelique Y. Chen, Xi |
author_facet | Santra, Abhishek Yu, Hai Tasnima, Nova Muthana, Musleh M. Li, Yanhong Zeng, Jie Kenyon, Nicholas J. Louie, Angelique Y. Chen, Xi |
author_sort | Santra, Abhishek |
collection | PubMed |
description | O-Sulfated sialyl Lewis x antigens play important roles in nature. However, due to their structural complexity, they are not readily accessible by either chemical or enzymatic synthetic processes. Taking advantage of a bacterial sialyltransferase mutant that can catalyze the transfer of different sialic acid forms from the corresponding sugar nucleotide donors to Lewis x antigens, which are fucosylated glycans, as well as an efficient one-pot multienzyme (OPME) sialylation system, O-sulfated sialyl Lewis x antigens containing different sialic acid forms and O-sulfation at different locations were systematically synthesized by chemoenzymatic methods. |
format | Online Article Text |
id | pubmed-5269574 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-52695742017-04-01 Systematic chemoenzymatic synthesis of O-sulfated sialyl Lewis x antigens Santra, Abhishek Yu, Hai Tasnima, Nova Muthana, Musleh M. Li, Yanhong Zeng, Jie Kenyon, Nicholas J. Louie, Angelique Y. Chen, Xi Chem Sci Chemistry O-Sulfated sialyl Lewis x antigens play important roles in nature. However, due to their structural complexity, they are not readily accessible by either chemical or enzymatic synthetic processes. Taking advantage of a bacterial sialyltransferase mutant that can catalyze the transfer of different sialic acid forms from the corresponding sugar nucleotide donors to Lewis x antigens, which are fucosylated glycans, as well as an efficient one-pot multienzyme (OPME) sialylation system, O-sulfated sialyl Lewis x antigens containing different sialic acid forms and O-sulfation at different locations were systematically synthesized by chemoenzymatic methods. Royal Society of Chemistry 2016-04-01 2015-12-17 /pmc/articles/PMC5269574/ /pubmed/28138383 http://dx.doi.org/10.1039/c5sc04104j Text en This journal is © The Royal Society of Chemistry 2016 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0) |
spellingShingle | Chemistry Santra, Abhishek Yu, Hai Tasnima, Nova Muthana, Musleh M. Li, Yanhong Zeng, Jie Kenyon, Nicholas J. Louie, Angelique Y. Chen, Xi Systematic chemoenzymatic synthesis of O-sulfated sialyl Lewis x antigens |
title | Systematic chemoenzymatic synthesis of O-sulfated sialyl Lewis x antigens
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title_full | Systematic chemoenzymatic synthesis of O-sulfated sialyl Lewis x antigens
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title_fullStr | Systematic chemoenzymatic synthesis of O-sulfated sialyl Lewis x antigens
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title_full_unstemmed | Systematic chemoenzymatic synthesis of O-sulfated sialyl Lewis x antigens
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title_short | Systematic chemoenzymatic synthesis of O-sulfated sialyl Lewis x antigens
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title_sort | systematic chemoenzymatic synthesis of o-sulfated sialyl lewis x antigens |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5269574/ https://www.ncbi.nlm.nih.gov/pubmed/28138383 http://dx.doi.org/10.1039/c5sc04104j |
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