Inhibition of Key Enzymes Linked to Obesity by Preparations From Mediterranean Dietary Plants: Effects on α-Amylase and Pancreatic Lipase Activities

One of the most important strategy in the treatment of obesity includes the development of nutrient digestion and absorption inhibitors. Inhibition of digestive enzymes is one of the most widely studied mechanisms used to determine the potential efficacy of natural products as hypolipidemic and hypoglycaemic agents. In vitro studies here reported were performed to evaluate the inhibitory activity of five species (as hydroalcoholic extracts) of edible plants from Calabria region (Italy) on amylase and lipase by monitoring the hydrolysis of p-NPC and the hydrolysis of glycoside bonds in digestible carbohydrate foods. The formulation obtained from Clematis vitalba L. exhibited the strongest inhibitory effect on pancreatic lipase (IC₅₀?=?0.99 mg/ml) and on α-amylase (IC₅₀?=?31.52 μg/ml). In order to explore metabolome production HPTLC analysis of the extracts was performed, revealing the predominance of (±)-catechin, caffeic acid and chlorogenic acid in C. vitalba formulation at concentration of 23.18?±?3.14, 13.63?±?0.65 and 18.88?±?0.76 mg/g, respectively. GC/MS analysis was used to identify fatty acids and terpene composition.     

Phallusiasterols A and B: Two New Sulfated Sterols from the Mediterranean Tunicate Phallusia fumigata and Their Effects as Modulators of the PXR Receptor

Purification of the apolar extracts of the marine ascidian Phallusia fumigata, afforded two new sulfated sterols, phallusiasterols A (1) and B (2). The structures of the new compounds have been elucidated using mass spectrometry and NMR experiments. The effects of phallusiasterols A and B as modulators of pregnane-X-receptor (PXR) have been investigated. These studies revealed that phallusiasterol A induces PXR transactivation in HepG2 cells and stimulates the expression of the PXR target genes CYP3A4 and MDR1 in the same cell line. Molecular docking calculations suggested the theoretical binding mode of phallusiasterol A with hPXR and revealed that phallusiasterol A fitted well in the LBD of PXR.