52116-51-5Relevant academic research and scientific papers
Tethered derivatives of d-glucose and pentacyclic triterpenes for homo/heterobivalent inhibition of glycogen phosphorylase
Cheng, Keguang,Liu, Jun,Sun, Hongbin,Bokor, Eva,Czifrak, Katalin,Konya, Balint,Toth, Marietta,Docsa, Tibor,Gergely, Pal,Somsak, Laszlo
, p. 1450 - 1464 (2010/09/16)
Propargyl esters of the C-28 carboxylic acids of pentacyclic triterpenes (oleanolic, ursolic, and maslinic acids) were coupled with 2,3,4,6-tetra-O- acetyl-β-d-glucopyranosyl azide as well as N-(ω-azido-[C-2, C-6, and C-11]alkanoyl)-β-d-glucopyranosylamines under conditions of copper(i)-catalyzed azide-alkyne cycloaddition (CuAAC) to give tethered d-glucose-triterpene heteroconjugates. The O-acetyl protecting groups were removed by base-catalyzed hydrolysis. N-(ω-Azido-[C-2, C-6, C-11, and C-16]alkanoyl)-β-d-glucopyranosylamines were also tethered by 1,7-octadiyne under CuAAC conditions to furnish d-glucose homoconjugates. O-Deacetylation was carried out by the Zemplen protocol. The new compounds were assayed against rabbit muscle glycogen phosphorylase (RMGP) a or b enzymes. Some of the heteroconjugates inhibited the enzyme in the low micromolar range (IC 50 values 40-70 μM), while the homoconjugates proved inefficient as inhibitors.
Synthesis and characterisation of poly (L-lactic acid) galactosyl derivatives; access to functionalised microspheres
Kassab, Rima,Fenet, Bernard,Fessi, Hatem,Parrot-Lopez, Hélène
, p. 877 - 881 (2007/10/03)
A new series of galactosyl-derived polymers has been used for the preparation of microspheres. The strategy is based on the modification of the terminal carboxylic group L-PLA (73.000) by coupling to a galactosyl antenna in the presence of the peptide coupling agents: DCC/HOBT. The degree of functionalisation varies between 60 and 70%, and antenna density between 1.74 and 2.78. The characterisations of the new products were carried out using 1H NMR, gel permeation chromatography, and acid base titration; the size of the functionalised microspheres was determined to be 210-270 μm by DLS. (C) 2000 Elsevier Science Ltd.
PURIFICATION AND PROPERTIES OF A β-D-MANNOSIDE MANNOHYDROLASE FROM GUAR
McClearly, Barry V.
, p. 75 - 92 (2007/10/02)
A β-D-mannoside mannohydrolase enzyme has been purified to homogeneity from germinated guar-seeds.Difficulties associated with the extraction and purification appeared to be due to an interaction of the enzyme with other protein material.The purified enzyme hydrolysed various natural and synthetic substrates, including β-D-manno-oligosaccharides and reduced β-D-manno-oligosaccharides of degree of polymerisation 2 to 6, as well as p-nitrophenyl, naphthyl, and methylumbelliferyl β-D-mannopyranosides.The preferred, natural substrate was β-D-mannopentaose, which was hydrolysed at twice the rate of β-D-mannotetraose and five times the rate of β-D-mannotriose.This result, together with the observation that α-D-mannose is released on hydrolysis, indicates that the enzyme is an exo-β-D-mannanase.
