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Synthetic Glycoforms Reveal Carbohydrate‐Dependent Bioactivity of Human Saposin D
Author(s) -
Graf Christopher G. F.,
Schulz Christian,
Schmälzlein Marina,
Heinlein Christian,
Mönnich Manuel,
Perkams Lukas,
Püttner Markus,
Boos Irene,
Hessefort Markus,
Lombana Sanchez Jose Nelson,
Weyand Michael,
Steegborn Clemens,
Breiden Bernadette,
Ross Kerstin,
Schwarzmann Günter,
Sandhoff Konrad,
Unverzagt Carlo
Publication year - 2017
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201701362
Subject(s) - glycan , biochemistry , glycoprotein , carbohydrate , chemistry , moiety , native chemical ligation , stereochemistry , cysteine , enzyme
The main glycoforms of the hydrophobic lysosomal glycoprotein saposin D (SapD) were synthesized by native chemical ligation. An approach for the challenging solid‐phase synthesis of the fragments was developed. Three SapD glycoforms were obtained following a general and robust refolding and purification protocol. A crystal structure of one glycoform confirmed its native structure and disulfide pattern. Functional assays revealed that the lipid‐binding properties of three SapD glycoforms are highly affected by the single sugar moiety of SapD showing a dependency of the size and the type of N‐glycan.