Thelephoric acid and kynapcin-9 in mushroom Polyozellus multiflex inhibit prolyl endopeptidase in vitro

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Thelephoric acid and kynapcin-9 in mushroom Polyozellus multiflex inhibit prolyl endopeptidase in vitro
Ju Yeon Kwak; In Koo Rhee; Kyung Bok Lee; Ji Sook Hwang; Ick Dong Yoo; Kyung Sik Song
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 9, no. 6, pp. 798-803
Publication Year
Prolyl endopeptidase [PEP; EC], a serine protease which is known to cleave peptide bonds on the carboxy side of a proline residue, plays an important role in the degradation of proline-containing neuropeptides that have been suggested to participate in learning and memory processes. An abnormal increase in the level of PEP, which can lead to generation of Aβ, is also suggested to be involved in Alzheimer's type senile dementia. In the course of screening PEP inhibitors from Basidiomycetes, the mushroom Polyozellus multiplex exhibited a high inhibitory activity against PEP. Two active compounds were isolated from the ethyl acetate soluble fraction by consecutive purification, using silica gel, Sephadex LH-20, and Lobar RP-18 chromatography. The chemical structures of these compounds were identified as thelephoric acid and 12-acetyl-2,3,7,8-tetrahydroxy-[12H]12- hydroxymethylbenzobis[1.2b,3.4b'] benzofuran-11-one (kynapcin-9) by spectral data including UV, IR, MS, HR-MS, 'H-, 13C-, and 2D-NMR. The IC50 values of the thelephoric acid and kynapcin-9 were 0.157 ppm (446 nM) and 0.087 ppm (212 nM) and their inhibitor constants (K1) were 0.73 ppm (2.09 μM) and 0.060 ppm (146 nM), respectively. Furthermore, they were non-competitive with a substrate in Dixon plots.
Prolyl endopeptidaseinhibitorPolyozellus multiflexthelephoric acid12-acetyl-2,3,7,8-tetrahydroxy[12H]-12-hydroxymethylbenzobis[1.2b,3.4b] benzofuran- 11-one (Kynapcin-9)
Korea Soc-Assoc-Inst
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