Anticonvulsant compounds from the wood of Caesalpinia sappan L.
80% Aqueous MeOH extracts from the wood of Caesalpinia sappan, which showed remarkable anticonvulsant activity, were fractionated using EtOAc, n-BuOH, and H2O. Among them, the EtOAc fraction significantly inhibited the activities of two GABA degradative enzymes, succinic semialdehyde dehydrogenase (SSADH) and succinic semialdehyde reductase (SSAR). Repeated column chromatographies for the fraction guided by activity test led to the isolation of the two active principal components. Their chemical structures were determined to be sappanchalcone and brazilin based on spectral data. The pure compounds, sappanchalcone (1) and brazilin (2), inactivated the SSAR activities in a dose dependent manner, whereas SSADH was inhibited partially by sappanchalcone and not by brazilin.
Baek
N I
NI
Department of Life Sciences, Kyunghee University, Suwon, Korea. nibaek@nms.kyunghee.ac.kr
Jeon
S G
SG
Ahn
E M
EM
Hahn
J T
JT
Bahn
J H
JH
Jang
J S
JS
Cho
S W
SW
Park
J K
JK
Choi
S Y
SY
D000445:Aldehyde Oxidoreductases / Q000037:antagonists & inhibitors; D000818:Animals; D000927:Anticonvulsants / Q000302:isolation & purification*; D002417:Cattle; D004791:Enzyme Inhibitors / Q000302:isolation & purification; D006884:Hydroxybutyrate Dehydrogenase / Q000037:antagonists & inhibitors; D010946:Plants, Medicinal / Q000737:chemistry*; D050644:Succinate-Semialdehyde Dehydrogenase; D014934:Wood
D000927:Anticonvulsants; D004791:Enzyme Inhibitors; D006884:Hydroxybutyrate Dehydrogenase; C019416:4-hydroxybutyrate dehydrogenase; D000445:Aldehyde Oxidoreductases; D050644:Succinate-Semialdehyde Dehydrogenase