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Cuparane sesquiterpenes from Laurencia natalensis Kylin as inhibitors of alpha-glucosidase, dipeptidyl peptidase IV and xanthine oxidase

Rengasamy, Kannan R.R., Slavětínská, Lenka Poštová, Kulkarni, Manoj G., Stirk, Wendy A., Van Staden, Johannes
Algal research 2017 v.25 pp. 178-183
Laurencia, algae, alpha-glucosidase, chromatography, dipeptidyl-peptidase IV, drugs, enzyme inhibition, enzyme inhibitors, nuclear magnetic resonance spectroscopy, physicochemical properties, prisms, sesquiterpenoids, silica, solvents, xanthine oxidase
The unexplored southern African red marine alga Laurencia natalensis was studied in a search for new enzyme inhibitors. A new cuparane sesquiterpenoid, 8-deoxyalgoane (1) along with two known sesquiterpenoids namely 1-deacetoxyalgoane (2) and algoane (3) were isolated from the MeOH:DCM extract using silica column chromatography with an hexane:EtOAc solvent system. Algoane was obtained as colourless prisms and structures of the three compounds were confirmed by NMR. The three compounds were tested for enzyme inhibitory activities against alpha-glucosidase and dipeptidyl peptidase IV (DPP-IV). Algoane was also tested against xanthine oxidase. In addition, molecular properties were determined to establish drug likeness, and other physico-chemical properties. This is the first report on the chemistry and biological properties of L. natalensis.