1. A prolyl endopeptidase-inhibiting benzofuran dimer from Polyozellus multiflex.
- Author
-
Song KS and Raskin I
- Subjects
- Bacterial Proteins, Benzofurans chemistry, Benzofurans pharmacology, Chromatography, Thin Layer, Chymotrypsin antagonists & inhibitors, Enzyme-Linked Immunosorbent Assay, Inhibitory Concentration 50, Korea, Molecular Conformation, Molecular Structure, Nuclear Magnetic Resonance, Biomolecular, Pancreatic Elastase antagonists & inhibitors, Prolyl Oligopeptidases, Serine Proteinase Inhibitors chemistry, Serine Proteinase Inhibitors pharmacology, Substrate Specificity, Trypsin Inhibitors chemistry, Trypsin Inhibitors isolation & purification, Trypsin Inhibitors pharmacology, Agaricales chemistry, Benzofurans isolation & purification, Serine Endopeptidases metabolism, Serine Proteinase Inhibitors isolation & purification
- Abstract
A new benzofuran dimer, 5,6,5',6'-tetrahydroxy[3,3']bibenzofuranyl-2,2'-dicarboxylic acid dimethyl ester (kynapcin-24), was isolated from Polyozellus multiflex and shown to noncompetitively inhibit prolyl endopeptidase (PEP), with an IC(50) value of 1.14 microM. Kynapcin-24 was less inhibitory to other serine proteases such as chymotrypsin, trypsin, and elastase.
- Published
- 2002
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