20298-35-5Relevant articles and documents
SYNTHESES OF 2-O-GLYCOSYL DERIVATIVES OF N-ACETYL-D-NEURAMINIC ACID
Ogura, Haruo,Furuhata, Kimio,Itoh, Masayoshi,Shitori, Yoshiyasu
, p. 37 - 52 (1986)
Syntheses of N-acetyl-D-neuraminic acid derivatives are reported.Methyl 4,7,8,9-tetra-O-acetyl-N-acetyl-2-chloro-2-deoxy-β-D-neuraminate (3) was prepared directly from methyl N-acetyl-β-D-neuraminate (2) in good yield.Koenigs-Knorr reaction of 3 with an excess of methanol gave the methyl α-glycoside of methyl N-acetyl-D-neuraminate (4). 2,3-O-Isopropylidene-D-ribono-1,4-lactone, 2,3-O-isopropylideneuridine, and 5-fluor-2,3-O-isopropylideneuridine reacted with 3 to give anomeric mixtures of methyl N-acetyl-D-neuraminate derivatives.The stereochemistry of these compounds was confirmed from n.m.r. and c.d. spectra, and measurements of the rate of hydrolysis of the glycosidic bond.
Revealing Functional Significance of Interleukin-2 Glycoproteoforms Enabled by Expressed Serine Ligation
Cao, Qi,Li, Bin,Liu, Jiazhi,Liu, Lizhen,Liu, Xinnan,Shao, Hong,Tao, Houchao,Wang, Can,Wang, Ping,Xue, Dongxiang,Ye, Farong,Yu, Biao,Zhao, Hongbo,Zhao, Jie
supporting information, (2022/01/31)
Naturally occurring interleukin-2 (IL-2) is a pleiotropic glycoprotein that regulates immune responses by controlling the differentiation and homeostasis of T cells. Non-glycosylated IL-2 has been used in clinical settings for three decades. However, the function of the O-glycan of native IL-2 remains elusive. Herein, to stress this issue, we report a highly efficient semi-synthesis of homogeneous glycosylated IL-2 with various glycoproteoforms on a multi-milligram scale. The glycopeptide fragment was prepared by chemical synthesis and then merged with recombinant fragment via a serine ligation to generate the desired glycoprotein in a single operation. Biological evaluation of the homogenous glycoprotein library reveals that the activity of IL-2 in activating individual T cell subset is glycan dependent, thus highlighting the possibility of further improving current clinical medicine.
Cooperative Multipoint Recognition of Sialic Acid by Benzoboroxole-Based Receptors Bearing Cationic Hydrogen-Bond Donors
Di Pasquale, Alice,Tommasone, Stefano,Xu, Lili,Ma, Jing,Mendes, Paula M.
, p. 8330 - 8338 (2020/07/17)
Sialic acid recognition remains an interesting and challenging target in molecular receptor design. Herein, we report a series of benzoboroxole-based receptors in which cationic hydrogen-bond donors have been introduced and shown to promote multipoint sialic acid recognition. One striking feature revealed by these receptors is that the carboxylate sialic acid residue is the primary binding determinant for recognition by benzoboroxole, in which the presence of charge-reinforced hydrogen bonds results in enhanced selectivity for sialic acid over other carbohydrates and a 4.5-fold increase in affinity. These findings open up wide possibilities for benzoboroxole-based receptors use in life science research, biotechnology, and diagnostics.
