kynapcin-13 and -28, new benzofuran prolyl endopeptidase inhibitors from polyozellus multiplex.
Two new benzofurans, 5,6-dihydroxybenzofuran-2,3-dicarboxylic acid dimethyl ester (kynapcin-13) and 5,6,5',6'-tetrahydroxy[3,3']bibenzofuranyl-2,2'-dicarboxylic acid 2'-methyl ester (kynapcin-28) were isolated from Polyozellus multiplex, and shown to non-competitively inhibit prolyl endopeptidase (PEP), with the IC50 values of 76.80 and 0.98 microM, respectively. Kynapcin-13 and -28 were less inhibitory to other serine proteases such as chymotrypsin, trypsin, and elastase.
Kim
Sang-In
SI
Division of Applied Biology and Chemistry, College of Agriculture and Life Sciences, Kyungpook National University, Daegu, Korea.
Park
In-Hye
IH
Song
Kyung-Sik
KS
D000363:Agaricales / Q000737:chemistry*; D001572:Benzofurans / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D004952:Esters / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D020128:Inhibitory Concentration 50; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases / Q000187:drug effects*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D001572:Benzofurans; D004952:Esters; D015842:Serine Proteinase Inhibitors; C466779:kynapcin-13; C466780:kynapcin-28; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases