Sugar nucleotides are essential glycosylation donors in the carbohydrate metabolism. Naturally, most sugar nucleotides are derived from a limited number of common sugar nucleotides by de novo biosynthetic pathways, undergoing single or multiple reactions such as dehydration, epimerization, isomerization, oxidation, reduction, amination, and acetylation reactions. However, it is widely believed that such complex bioconversions are not practical for synthetic use due to the high preparation cost and great difficulties in product isolation. Therefore, most of the discovered sugar nucleotides are not readily available. Here, based on de novo biosynthesis mainly, 13 difficult-to-access sugar nucleotides were successfully prepared from two common sugars D-Man and sucrose in high yields, at a multigram scale, and without the need for tedious purification manipulations. This work demonstrated that de novo biosynthesis, although undergoing complex reactions, is also practical and cost-effective for synthetic use by employing a cascade conversion strategy.

Bi3+ -TiO 2 photocatalysts were prepared by doping bismuth ion into the TiO 2 structure in a sol-gel process. The catalyst samples were then characterized by UV-vis diffuse reflectance spectra (DRS), X-ray photoelectron spectroscopy (XPS), Fourier transform infrared spectroscopy (FT-IR), X-ray diffraction (XRD) and transmission electron microscopy (TEM). Rodamine-B (RhB) was used in this study as a model chemical with the aim of organic pollutants control. The photocatalytic degradation of RhB demonstrated that an optimal loading of bismuth 0.7 at. % achieved the highest photodegradation rate, with the rate constant increasing by a factor of 3.89 over neat TiO 2 (P25) under UV illumination (k ≥ 320 nm). The degradation of p-nitrobenzonic acid (pNBA) was also examined to prevent/preclude/exclude/ the photosensitization pathway. GC-MS results show that pNBA can be effectively degraded and minerized to small molecules, such as quinone, acetic acid and formic acid.

Core fucosylation, the attachment of α1,6fucose to the innermost N-acetylglucosamine (GlcNAc) residue of N-glycans, has a strong relationship with tumor growth, invasion, metastasis, prognosis, and immune evasion by regulating many membrane proteins. However, details about the functional mechanism are still largely unknown due to the lack of an effective analytical method to identify cell-surface core-fucosylated glycoproteins, and especially glycosylation sites.Here, we developed a sensitive and reversible labeling strategy for probing core fucosylation, by which corefucosylated glycoproteins that located on cell-surface were selectively tagged by a biotinylated probe with high sensitivity. The labeled probe can be further broken enzymatically after the capture by affinity resin. The on-bead traceless cleavage allowed the global mapping of core-fucosylated glycoproteins and glycosylation sites by mass spectrometry (MS). The profile of core-fucosylated glycoproteome provides an in-depth understanding of the biological functions of core fucosylation.