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KMID : 0385520110240020135
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Analytical Science & Technology
2011 Volume.24 No. 2 p.135 ~ p.141
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A study of matrix metalloproteinase-9 inhibitor in Hovenia dulcis Thunberg
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Kim Eun-Ho
Lee Kwang-Soo
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Abstract
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MMPs (Matrix metalloproteinases) are enzymes playing an important role to turnover and remodel main protein compositions of extracellular matrix. MMP-2 and MMP-9 of MMPs having a catalytic domain which is apart from a hemopexin-like domain part, are different from the other MMPs pertaining fibronectinlike domain close to hemopexin-like domain. It was reported that the development of MMP-9 restrainer can prevent the transfer of liver cancer. In this study, MMP-9 restrainers were extracted and purified from Hovenia dulcis Thunberg. The each fractionary part was examined to investigate the inhibitory effect on MMPs. Three compounds, compound A and B eluted with ethyl acetate (EA) and compound C with methanol, were identified by ¹H and ¹³C NMR, GC/MS, and FT-IR. Compound A is considered as a kind of catechine type compound having a benzene ring substituted by hydroxyl and methoxyl groups. Compound B and C are nobiletin type compound pertaining a carbonyl group. Compound A, B and C showed 76%, 66% and 71% of inhibition effect on MMP-9 at 1.0% concentration, respectively. Compound A showed the best inhibition effect on MMP-9.
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KEYWORD
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Hovenia dulcis Thunberg, MMPs, GC/MS, IR, NMR, Nobiletin
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