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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Agaricales / chemistry*
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Bacterial Proteins
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Benzofurans / chemistry
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Benzofurans / isolation & purification*
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Benzofurans / pharmacology
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Chromatography, Thin Layer
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Chymotrypsin / antagonists & inhibitors
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Enzyme-Linked Immunosorbent Assay
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Inhibitory Concentration 50
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Korea
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Molecular Conformation
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Molecular Structure
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Nuclear Magnetic Resonance, Biomolecular
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Pancreatic Elastase / antagonists & inhibitors
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Prolyl Oligopeptidases
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Serine Endopeptidases / metabolism*
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Serine Proteinase Inhibitors / chemistry
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Serine Proteinase Inhibitors / isolation & purification*
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Serine Proteinase Inhibitors / pharmacology
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Substrate Specificity
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Trypsin Inhibitors / chemistry
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Trypsin Inhibitors / isolation & purification
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Trypsin Inhibitors / pharmacology
Substances
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Bacterial Proteins
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Benzofurans
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Serine Proteinase Inhibitors
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Trypsin Inhibitors
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kynapcin-24
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flavobacterin protein, Flavobacterium aquatile
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Serine Endopeptidases
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Chymotrypsin
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Prolyl Oligopeptidases
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Pancreatic Elastase