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Published on: June 18, 2020
Redox-Controlled Site-Specific α2-6-Sialylation
Na Lu1, Jinfeng Ye1, Jiansong Cheng2
1National Glycoengineering Research Center, State Key Laboratory of Microbial Technology , Shandong University , Qingdao 266237 , China.
Abstract:
The first bacterial α2-6-sialyltransferase cloned from Photobacterium damselae (Pd2,6ST) has been widely applied for the synthesis of various α2-6-linked sialosides. However, the extreme substrate flexibility of Pd2,6ST makes it unsuitable for site-specific α2-6-sialylation of complex substrates containing multiple galactose and/or N-acetylgalactosamine units. To tackle this problem, a general redox-controlled site-specific sialylation strategy using Pd2,6ST is described. This approach features site-specific enzymatic oxidation of galactose units to mask the unwanted sialylation sites and precisely controlling the site-specific α2-6-sialylation at intact galactose or N-acetylgalactosamine units.
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