20818-25-1Relevant articles and documents
β-D-glucosyl and α-D-galactosyl yariv reagents: Syntheses from p-nitrophenyl-D-glycosides by transfer reduction using ammonium formate
Basile, Dominick V.,Ganjian, Iraj
, p. 7453 - 7456 (2004)
Yariv β-D-glucosyl (4a) and Yariv α-D-galactosyl (4b) reagents are multivalent phenylglycosides. The β-D-glucosyl reagent is considered diagnostic for arabinogalactan proteins (AGPs) to which it can reversibly bind, stain, and precipitate. The α-D-galacto
Molecularly Imprinted Synthetic Glucosidase for the Hydrolysis of Cellulose in Aqueous and Nonaqueous Solutions
Li, Xiaowei,Zangiabadi, Milad,Zhao, Yan
, p. 5172 - 5181 (2021)
Molecular imprinting is a powerful and yet simple method to create multifunctional binding sites within a cross-linked polymer network. We report a new class of synthetic glucosidase prepared through molecular imprinting and postfunctionalization of cross-linked surfactant micelles. These catalysts are protein-sized water-soluble nanoparticles that can be modified in multiple ways. As their natural counterparts, they bind a glucose-containing oligo- or polysaccharide. They contain acidic groups near the glycosidic bond to be cleaved, with the number and distance of the acid groups tuned systematically. Hydrolysis of cellulose in a key step in biomass conversion but is hampered by the incalcitrance of the highly crystalline cellulose fibers. The synthetic glucosidases are shown to hydrolyze cellobiose and cellulose under a variety of conditions. The best catalyst, with a biomimetic double acid catalytic motif, can hydrolyze cellulose with one-fifth of the activity of commercial cellulases in aqueous buffer. As a highly cross-linked polymeric nanoparticle, the synthetic catalyst is stable at elevated temperatures in both aqueous and nonaqueous solvents. In a polar aprotic solvent/ionic liquid mixture, it hydrolyzes cellulose several times faster than commercial cellulases in aqueous buffer. When deposited on magnetic nanoparticles, it retains 75% of its activity after 10 cycles of usage.
Enzymatic Synthesis of a Series of Thioglycosides: Analogs of Arbutin with Efficient Antipigmentation Properties
Daniellou, Richard,Didak, Blanka,Guillotin, Laure,Lafite, Pierre,Landemarre, Ludovic,Lemiègre, Lo?c,Peyrot, Cédric
, p. 3812 - 3818 (2021/08/24)
Arbutin, a natural glycoside, is well known as a commercial tyrosinase inhibitor, and thus, to prevent pigmentary disorders of skin. In fact, tyrosinase is involved in the biosynthesis of melanin, the skin main pigment. However, arbutin is subject to hydr
Rapid phenolic O-glycosylation of small molecules and complex unprotected peptides in aqueous solvent
Wadzinski, Tyler J.,Steinauer, Angela,Hie, Liana,Pelletier, Guillaume,Schepartz, Alanna,Miller, Scott J.
, p. 644 - 652 (2018/05/04)
Glycosylated natural products and synthetic glycopeptides represent a significant and growing source of biochemical probes and therapeutic agents. However, methods that enable the aqueous glycosylation of endogenous amino acid functionality in peptides without the use of protecting groups are scarce. Here, we report a transformation that facilitates the efficient aqueous O-glycosylation of phenolic functionality in a wide range of small molecules, unprotected tyrosine, and tyrosine residues embedded within a range of complex, fully unprotected peptides. The transformation, which uses glycosyl fluoride donors and is promoted by Ca(OH)2, proceeds rapidly at room temperature in water, with good yields and selective formation of unique anomeric products depending on the stereochemistry of the glycosyl donor. High functional group tolerance is observed, and the phenol glycosylation occurs selectively in the presence of virtually all side chains of the proteinogenic amino acids with the singular exception of Cys. This method offers a highly selective, efficient, and operationally simple approach for the protecting-group-free synthesis of O-aryl glycosides and Tyr-O-glycosylated peptides in water.
