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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.