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Exploration of human xylosyltransferase for chemoenzymatic synthesis of proteoglycan linkage region
Author(s) -
Jia Gao,
Peng Lin,
Setare Tahmasebi Nick,
Kunli Liu,
Kefei Yu,
Erhard Hohenester,
Xuefei Huang
Publication year - 2021
Publication title -
organic and biomolecular chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 146
eISSN - 1477-0539
pISSN - 1477-0520
DOI - 10.1039/d1ob00317h
Subject(s) - proteoglycan , chemistry , glycan , glycopeptide , glycosaminoglycan , biochemistry , glycoprotein , xylose , glycosylation , peptide , glycobiology , stereochemistry , extracellular matrix , fermentation , antibiotics
Proteoglycans (PGs) play important roles in many biological processes including tumor progression, cell adhesion, and regulation of growth factor activities. With glycosaminoglycan chains attached to the core proteins in nature, PGs are highly challenging synthetic targets due to the difficulties in integrating the sulfated glycans with the peptide backbone. To expedite the synthesis, herein, the utility of human xylosyltransferase I (XT-I), the enzyme responsible for initiating PG synthesis, has been explored. XT-I was found to be capable of efficiently installing the xylose unit onto a variety of peptide structures on mg scales. Furthermore, an unnatural sugar, i.e., 6-azidoglucose can be transferred by XT-I introducing a reactive handle onto the glycopeptide for selective functionalization. XT-I can be coupled with β-4-galactosyl transferase-7 for one pot synthesis of glycopeptides bearing galactose-xylose disaccharide, paving the way toward efficient chemoenzymatic synthesis of PG glycopeptides and glycoproteins.

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