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  Automated glycan assembly of oligosaccharides related to arabinogalactan proteins

Bartetzko, M., Schuhmacher, F., Hahm, H. S., Seeberger, P. H., & Pfrengle, F. (2015). Automated glycan assembly of oligosaccharides related to arabinogalactan proteins. Organic Letters, 17(17), 4344-4347. doi:10.1021/acs.orglett.5b02185.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-492B-8 Version Permalink: http://hdl.handle.net/21.11116/0000-0006-59E6-3
Genre: Journal Article

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 Creators:
Bartetzko, Max1, Author              
Schuhmacher, Frank2, Author              
Hahm, Heung Sik2, Author              
Seeberger, Peter H.2, Author              
Pfrengle, Fabian1, Author              
Affiliations:
1Fabian Pfrengle, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863303              
2Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863306              

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 Abstract: Arabinogalactan proteins are heavily glycosylated proteoglycans in plants. Their glycan portion consists of type-II arabinogalactan polysaccharides whose heterogeneity hampers the assignment of the arabinogalactan protein function. Synthetic chemistry is key to the procurement of molecular probes for plant biologists. Described is the automated glycan assembly of 14 oligosaccharides from four monosaccharide building blocks. These linear and branched glycans represent key structural features of natural type-II arabinogalactans and will serve as tools for arabinogalactan biology.

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 Dates: 2015-08-212015
 Publication Status: Published in print
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 Identifiers: DOI: 10.1021/acs.orglett.5b02185
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Title: Organic Letters
  Other : Org. Lett.
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 17 (17) Sequence Number: - Start / End Page: 4344 - 4347 Identifier: ISSN: 1523-7060