%0 Journal Article
%T Analyzing the Interaction of Andrographolide and Neoandrographolide, Diterpenoid Compounds From Andrographis Paniculata (Burm.F) Nees, to Cyclooxygenase-2 Enzyme by Docking Simulation
%A Jutti Levita
%A Enade P. Istyastono
%A As¡¯ari Nawawi
%A Abdul Mutholib
%J ITB Journal of Science
%D 2009
%I 
%X Cyclooxygenase (COX), an enzyme involved in the conversion of arachidonic acid to prostaglandins, exists in two isoforms, which are COX-1 and COX-2. Despite the similarities of COX-1 and COX-2, the two isoforms show subtle differences in amino acid composition at the active sites. Since COX-1 has isoleucine, a bulkier amino acid at position 523 than COX-2¡¯s valine, it allows COX-2 to have a larger space in its active site. Andrographolide reduces COX-2 expression induced by PAF and fMLP in HL60/neutrophils. Neoandrographolide inhibits COX-2 expression at the translational level. The purpose of this study is to examine the binding modes of andrographolide and neoandrographolide against COX-1 and COX-2 in terms of hydrogen bonds and docking energy, to understand their antiinflammatory property. The docking study indicates that both andrographolide and neoandrographolide are able to be located in the COX-2¡¯s binding pocket but not in the COX-1¡¯s. It confirms that COX-1¡¯s binding pocket is smaller than COX-2¡¯s. Based on this study, both andrographolide and neoandrographolide show selective inhibitory property to COX-2. Their selectivity are due to their specific interaction with Arg 513 in the binding pocket of COX-2, which is also shown by SC-558, a COX-2 selective inhibitor.
%K COX
%K andrographolide
%K neoandrographolide
%K docking simulation
%U http://journal.itb.ac.id/download.php?file=A09018.pdf&id=350&up=10