TY - JOUR
T1 - Xanthones with pancreatic lipase inhibitory activity from the pericarps of Garcinia mangostana L. (Guttiferae)
AU - Chae, Hee Sung
AU - Kim, Eun Young
AU - Han, Ling
AU - Kim, Na Rae
AU - Lam, Bunthoeun
AU - Paik, Jin Hyub
AU - Yoon, Kee Dong
AU - Choi, Young Hee
AU - Chin, Young Won
N1 - Publisher Copyright:
© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
PY - 2016/9/1
Y1 - 2016/9/1
N2 - Bioactivity-guided isolation of natural compounds from the pericarps of Garcinia mangostana, using a pancreatic lipase assay, led to the identification of 13 xanthones including α-mangostin (1), β-mangostin (2), γ-mangostin (3), 1-isomangostin (4), gartanin (5), garcinone D (6), 9-hydroxycalabaxanthone (7), smeathxanthone A (8), tovophyllin A (9), 8- deoxygartanin (10), mangostanin (11), calocalabaxanthone (12), and 1,7-dihydroxy-3-methoxy-2-(3-methylbut-2-enyl) xanthen-9-one (13). The inhibitory activities of the isolated xanthones against pancreatic lipase were evaluated and α-mangostin (1) was found to possess the most potent inhibitory activity (IC50 5.0 µM) in a non-competitive manner, compared with the positive control, orlistat (IC50 3.9 µM). Practical applications: Pancreatic lipase is a key enzyme in lipid absorption. A total of 13 compounds were isolated from the pericarps of G. mangostana. Their structures were characterized by HRESI-MS, and 1D and 2D-NMR spectroscopic data. Our results show that all the isolates exhibited inhibitory activity against pancreatic lipase. Of the active xanthones, α-mangostin displayed the most potent lipase inhibition, with an IC50 value of 5.0 μM. Furthermore, kinetic analysis of α-mangostin was carried out. In the Lineweaver–Burk plot, the apparent Vmax values in the presence of 1, 2, 4, and 10 µM α-mangostin were decreased compared with those without α-mangostin, whereas the Km values of 4-MU oleate with and without α-mangostin were both close to 3.22 μM. Finally, it is evident that xanthone derivatives isolated from G. mangostana possess pancreatic lipase inhibitory activities. A total of 13 compounds are isolated from the pericarps of Garcinia mangostana. α-Mangostin is found to possess the most potent lipase inhibitory activity.
AB - Bioactivity-guided isolation of natural compounds from the pericarps of Garcinia mangostana, using a pancreatic lipase assay, led to the identification of 13 xanthones including α-mangostin (1), β-mangostin (2), γ-mangostin (3), 1-isomangostin (4), gartanin (5), garcinone D (6), 9-hydroxycalabaxanthone (7), smeathxanthone A (8), tovophyllin A (9), 8- deoxygartanin (10), mangostanin (11), calocalabaxanthone (12), and 1,7-dihydroxy-3-methoxy-2-(3-methylbut-2-enyl) xanthen-9-one (13). The inhibitory activities of the isolated xanthones against pancreatic lipase were evaluated and α-mangostin (1) was found to possess the most potent inhibitory activity (IC50 5.0 µM) in a non-competitive manner, compared with the positive control, orlistat (IC50 3.9 µM). Practical applications: Pancreatic lipase is a key enzyme in lipid absorption. A total of 13 compounds were isolated from the pericarps of G. mangostana. Their structures were characterized by HRESI-MS, and 1D and 2D-NMR spectroscopic data. Our results show that all the isolates exhibited inhibitory activity against pancreatic lipase. Of the active xanthones, α-mangostin displayed the most potent lipase inhibition, with an IC50 value of 5.0 μM. Furthermore, kinetic analysis of α-mangostin was carried out. In the Lineweaver–Burk plot, the apparent Vmax values in the presence of 1, 2, 4, and 10 µM α-mangostin were decreased compared with those without α-mangostin, whereas the Km values of 4-MU oleate with and without α-mangostin were both close to 3.22 μM. Finally, it is evident that xanthone derivatives isolated from G. mangostana possess pancreatic lipase inhibitory activities. A total of 13 compounds are isolated from the pericarps of Garcinia mangostana. α-Mangostin is found to possess the most potent lipase inhibitory activity.
KW - Alpha-mangostin
KW - Garcinia mangostana
KW - Orlistat
KW - Pancreatic lipase
UR - http://www.scopus.com/inward/record.url?scp=84954305514&partnerID=8YFLogxK
U2 - 10.1002/ejlt.201500516
DO - 10.1002/ejlt.201500516
M3 - Article
AN - SCOPUS:84954305514
SN - 1438-7697
VL - 118
SP - 1416
EP - 1421
JO - European Journal of Lipid Science and Technology
JF - European Journal of Lipid Science and Technology
IS - 9
ER -