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Journal Article

Automated glycan assembly of oligosaccharides related to arabinogalactan proteins

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Bartetzko,  Max
Fabian Pfrengle, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Schuhmacher,  Frank
Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Hahm,  Heung Sik
Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Seeberger,  Peter H.
Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Pfrengle,  Fabian
Fabian Pfrengle, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Citation

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.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0028-492B-8
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.