52222-74-9

Usage

Uses

Used in Pharmaceutical Industry:
KaeMpferol-4'-O-β-D-glucopyranoside is used as a bioactive compound for its potential therapeutic properties. It has been studied for its antioxidant, anti-inflammatory, and anti-cancer activities, making it a promising candidate for the development of new drugs and treatments.
Used in Cosmetic Industry:
In the cosmetic industry, KaeMpferol-4'-O-β-D-glucopyranoside is used as an ingredient for its skin-friendly properties. It is valued for its antioxidant and anti-inflammatory effects, which can help protect the skin from environmental stressors and promote a healthy complexion.
Used in Functional Foods:
KaeMpferol-4'-O-β-D-glucopyranoside is also used in the development of functional foods and dietary supplements. Its antioxidant and anti-inflammatory properties can contribute to overall health and well-being when consumed as part of a balanced diet.
Used in Drug Delivery Systems:
Similar to gallotannin, KaeMpferol-4'-O-β-D-glucopyranoside can be incorporated into drug delivery systems to enhance its bioavailability and therapeutic outcomes. Researchers are exploring the use of various carriers, such as organic and metallic nanoparticles, to improve the delivery and efficacy of KaeMpferol-4'-O-β-D-glucopyranoside in treating specific health conditions.

InChI:InChI=1/C21H20O11/c22-7-13-15(25)17(27)19(29)21(32-13)30-10-3-1-8(2-4-10)20-18(28)16(26)14-11(24)5-9(23)6-12(14)31-20/h1-6,13,15,17,19,21-25,27-29H,7H2/t13-,15-,17+,19-,21-/m1/s1

Upstream product

• 520-18-3 kaempferol 
• 952585-00-1 uridine-5'-diphosphoglucose 
• 133-89-1 UDP-glucose 

Relevant academic research and scientific papers

Functional Characterization and Protein Engineering of a Triterpene 3-/6-/2′-O-Glycosyltransferase Reveal a Conserved Residue Critical for the Regiospecificity

Engineering the function of triterpene glucosyltransferases (GTs) is challenging due to the large size of the sugar acceptors. In this work, we identified a multifunctional glycosyltransferase AmGT8 catalyzing triterpene 3-/6-/2′-O-glycosylation from the medicinal plant Astragalus membranaceus. To engineer its regiospecificity, a small mutant library was built based on semi-rational design. Variants A394F, A394D, and T131V were found to catalyze specific 6-O, 3-O, and 2′-O glycosylation, respectively. The origin of regioselectivity of AmGT8 and its A394F variant was studied by molecular dynamics and hydrogen deuterium exchange mass spectrometry. Residue 394 is highly conserved as A/G and is critical for the regiospecificity of the C- and O-GTs TcCGT1 and GuGT10/14. Finally, astragalosides III and IV were synthesized by mutants A394F, T131V and P192E. This work reports biocatalysts for saponin synthesis and gives new insights into protein engineering of regioselectivity in plant GTs.

An Ambidextrous Polyphenol Glycosyltransferase PaGT2 from Phytolacca americana

The glycosylation of small hydrophobic compounds is catalyzed by uridine diphosphate glycosyltransferases (UGTs). Because glycosylation is an invaluable tool for improving the stability and water solubility of hydrophobic compounds, UGTs have attracted attention for their application in the food, cosmetics, and pharmaceutical industries. However, the ability of UGTs to accept and glycosylate a wide range of substrates is not clearly understood due to the existence of a large number of UGTs. PaGT2, a UGT from Phytolacca americana, can regioselectively glycosylate piceatannol but has low activity toward other stilbenoids. To elucidate the substrate specificity and catalytic mechanism, we determined the crystal structures of PaGT2 with and without substrates and performed molecular docking studies. The structures have revealed key residues involved in substrate recognition and suggest the presence of a nonconserved catalytic residue (His81) in addition to the highly conserved catalytic histidine in UGTs (His18). The role of the identified residues in substrate recognition and catalysis is elucidated with the mutational assay. Additionally, the structure-guided mutation of Cys142 to other residues, Ala, Phe, and Gln, allows PaGT2 to glycosylate resveratrol with high regioselectivity, which is negligibly glycosylated by the wild-type enzyme. These results provide a basis for tailoring an efficient glycosyltransferase.

Antitumor, antioxidant and anti-inflammatory activities of kaempferol and its corresponding glycosides and the enzymatic preparation of kaempferol

Kaempferol (kae) and its glycosides are widely distributed in nature and show multiple bio-activities, yet few reports have compared them. In this paper, we report the antitumor, antioxidant and anti-inflammatory activity differences of kae, kae-7-O-gluco

Antiviral composition derived from allium CEPA and therapeutic use thereof

Novel medicinal extracts derived from Allium species, preferablyAllium cepaare provided. These extracts have broad medicinal properties, especially for treatment of AIDS and other viral infections.