期刊
BIOORGANIC & MEDICINAL CHEMISTRY
卷 21, 期 16, 页码 4778-4785出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2013.02.040
关键词
Carbohydrate; Chemoenzymatic synthesis; Enzymatic synthesis; Glycopeptide; T antigen; Tn antigen; ST antigen; STn antigen
资金
- NIH [R01HD065122]
- NSF [CHE-1012511]
- Camille & Henry Dreyfus Foundation
- Direct For Mathematical & Physical Scien [1012511] Funding Source: National Science Foundation
- Division Of Chemistry [1012511] Funding Source: National Science Foundation
A series of STn-MUC1 and ST-MUC1 glycopeptides containing naturally occurring and non-natural sialic acids have been chemoenzymatically synthesized from Tn-MUC1 glycopeptide using one-pot multienzyme (OPME) approaches. In situ generation of the sialyltransferase donor cytidine 5'-monophosphate-sialic acid (CMP-Sia) using a CMP-sialic acid synthetase in the presence of an extra amount of cytidine 5'-triphosphate (CTP) and removal of CMP from the reaction mixture by flash C18 cartridge purification allow the complete consumption of Tn-MUC1 glycopeptide for quantitative synthesis of STn-MUC1. A Campylobacter jejuni beta 1-3GalT (CjCgtB Delta 30-His(6)) mutant has been found to catalyze the transfer of one or more galactose residues to Tn-MUC1 for the synthesis of T-MUC1 and galactosylated T-MUC1. Sialylation of T-MUC1 using Pasteurella multocida alpha 2-3-sialyltransferase 3 (PmST3) with Neisseria meningitidis acid synthetase (NmCSS) and Escherichia coli sialic acid aldolase in one pot produced ST-MUC1 efficiently. These glycopeptides are potential cancer vaccine candidates. (C) 2013 Elsevier Ltd. All rights reserved.
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