Chemoenzymatic synthesis of Neu5Ac9NAc-containing α2-3- and α2-6-linked sialosides and their use for sialidase substrate specificity studies.

ABSTRACT: O-Acetylation of sialic acid (Sia) modulates its recognition by sialic acid-binding proteins and plays an important role in biological and pathological processes. 9-O-Acetylation is the most common modification of sialic acid in human. However, study of O-acetylated sialoglycans is hampered due to the instability of O-acetyl group towards pH changes and sensitivity to esterases. Our previous studies demonstrated a chemical biology method to this problem by replacing the oxygen atom in the C9 ester group of sialic acid by a nitrogen to form an amide. Here, we synthesized a library of sixteen new 9-acetamido-9-deoxy-N-acetylneuraminic acid (Neu5Ac9NAc)-containing α2-3- and α2-6-linked sialosides with various underlying glycans using efficient one-pot three-enzyme (OP3E) sialylation systems.

SUBMITTER: Li W 

PROVIDER: S-EPMC5662470 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature