o-glcnacylation

OSMI-1 是一种 O-GlcNAc 转移酶 (OGT) 抑制剂 (IC50=2.7 μM)，具有口服活性和细胞渗透性。OSMI-1 可以抑制蛋白质 O-GlcNA 酰化，而不会定性地改变细胞表面 N- 或 O- 连接的聚糖。

O-GlcNAcase-IN-2（化合物81）是一种具口服活性、能穿透血脑屏障的OGA抑制剂，其IC50值为4.93 nM。该化合物能显著增加蛋白质的O-GlcNAcylation水平，并在OA损伤的SH-SY5Y细胞模型中降低tau蛋白的磷酸化状态（p-Ser199、p-Thr205和p-Ser396）。此外，O-GlcNAcase-IN-2还能改善APP PS1小鼠模型的认知功能，显示出其对抗阿兹海默症（AD）的潜力。

(Rac)-OSMI-1 是 OSMI-1 的外消旋体。其中 OSMI-1 是 O-GlcNAc 转移酶 (OGT) 抑制剂 (IC50: 2.7 μM)。OSMI-1 对哺乳动物细胞系中的蛋白 O-连接的 N-乙酰氨基葡萄糖 (O-GlcNAcylation) 具有抑制作用，且不会定性地改变细胞表面 N-或 O-连接的聚糖。

Histone H2B (108-125) is a peptide fragment of histone H2B that corresponds to amino acid residues 109-126 of the human histone H2B sequence. It contains an N-terminal biotinylated lysine followed by a tryptophan linker. Histone H2B can be modified by addition of an O-linked N-acetylglucosamine (GlcNAc) moiety to the serine residue at position 112, which promotes monoubiquitination of the lysine at position 120.1 Both of these modifications are associated with active transcription. Histone H2B also has lysine residues at positions 108, 116, and 120 that are subject to acetylation.2References1. Fujiki, R., Hashiba, W., Sekine, H., et al. GlcNAcylation of histone H2B facilitates its monoubiquitination. Nature 480(7378), 557-560 (2011).2. Portela, A., and Esteller, M. Epigenetic modifications and human disease. Nat. Biotechnol. 28(10), 1057-1068 (2010). Histone H2B (108-125) is a peptide fragment of histone H2B that corresponds to amino acid residues 109-126 of the human histone H2B sequence. It contains an N-terminal biotinylated lysine followed by a tryptophan linker. Histone H2B can be modified by addition of an O-linked N-acetylglucosamine (GlcNAc) moiety to the serine residue at position 112, which promotes monoubiquitination of the lysine at position 120.1 Both of these modifications are associated with active transcription. Histone H2B also has lysine residues at positions 108, 116, and 120 that are subject to acetylation.2 References1. Fujiki, R., Hashiba, W., Sekine, H., et al. GlcNAcylation of histone H2B facilitates its monoubiquitination. Nature 480(7378), 557-560 (2011).2. Portela, A., and Esteller, M. Epigenetic modifications and human disease. Nat. Biotechnol. 28(10), 1057-1068 (2010).