Human neutrophil elastase (HNE) inhibitory polyprenylated acylphloroglucinols from the flowers of Hypericum ascyron |
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| Institution: | 1. Division of Applied Life Science (BK21 plus), IALS, Gyeongsang National University, Jinju 52828, Republic of Korea;2. College of Food and Biological Engineering, Qiqihar University, Qiqihar 161006, China;1. Division of Applied Life Science (BK21 Plus), IALS, Gyeongsang National University, Jinju, 52828, Republic of Korea;2. PMBBRC, Gyeongsang National University, Jinju, 52828, Republic of Korea;1. School of Basic Medical Sciences, Guizhou Medical University, Guiyang 550025, China;2. State Key Laboratory of Functions and Applications of Medicinal Plants, Guizhou Medical University, Guiyang 550014, China;3. The Key Laboratory of Chemistry for Natural Products of Guizhou Province and Chinese Academy of Sciences, Guiyang 550014, China;4. State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Science, Kunming 650201, China;1. State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650201, Yunnan, PR China;2. Laboratory of Chinese Herbal Drug Discovery, Tropical Medicine Institute, Guangzhou University of Chinese Medicine, Guangzhou 510405, PR China;3. University of Chinese Academy of Sciences, Beijing 100049, PR China |
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| Abstract: | In the course of an investigation of human neutrophil elastase (HNE) associated with inflammation, the extract of the flower parts of Hypericum ascyron showed a significant influence to HNE. The responsible metabolites to HNE inhibition were found to be eight polyprenylated acylphloroglucinols, PPAPs (1–8) which showed IC50 ranges between 2.4 and 19.9 μM. This is the first report to demonstrate that PPAP skeleton exhibits potent HNE inhibition. The compounds 1–3 were characterized and newly named as ascyronone E (IC50 = 4.3 μM), ascyronone F (IC50 = 19.9 μM), ascyronone G (IC50 = 4.5 μM) based on 2D-NMR spectroscopic data. In the kinetic analysis of double reciprocal plots, all the compounds showed noncompetitive behaviors to HNE enzyme with the remaining of Km and the increase of Vmax. The binding affinity levels (KSV) by using fluorescence were sufficient to be able to prove that PPAPs (1–8) had compliant interaction with inhibitory potencies. |
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| Keywords: | Human neutrophil elastase Polycyclic polyprenylated acylphloroglucinols Enzyme kinetics |
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