3 beta-Hydroxysialic acid glycosides. I. Calcium-binding ability and chemical and enzymatic stabilities

• Published in: Chemical & pharmaceutical bulletin Vol. 40; no. 10; pp. 2728 - 2734
• Main Authors: Okamoto, K, Hasegawa, T, Toyomaki, Y, Yamakawa, M, Okukado, N
• Format: Journal Article
• Language: English
• Published: Japan 01.10.1992
• Subjects: Animals; Calcium - chemistry; Cattle; Enzyme Stability; Glycosides - chemistry; Hydrolysis; Magnetic Resonance Spectroscopy; Molecular Conformation; N-Acetylneuraminic Acid; Neuraminidase - chemistry; Sialic Acids - chemistry; Structure-Activity Relationship
• ISSN: 0009-2363

Methyl alpha- and beta-glycosides of N-acetylneuraminic acid (Neu5Ac) and N-acetyl-3 beta-hydroxyneuraminic acid (Neu5Ac beta 3OH) (1-4) were prepared to evaluate their calcium-binding ability. (Methyl alpha-glucopyranosidonyl) alpha- and beta-, and 4-methylumbelliferyl alpha-glycosides of Neu5Ac and Neu5Ac beta 3OH (5-10) were also synthesized for the comparison of chemical and enzymatic stabilities, respectively. Methyl beta-glycosides of Neu5Ac and Neu5Ac beta 3OH, 3 and 4, respectively, showed intense calcium-binding abilities, while no such ability was observed in the corresponding alpha-glycosides, 1 and 2. The Neu5Ac beta 3OH glycosides, 6, 8, and 10, showed much stronger resistance to acidic hydrolysis and sialidase digestion than the corresponding Neu5Ac glycosides, 5, 7, and 9.