Isolation and Identification of Monoamine Oxidase Inhibitory substances from the fruits of Crataegus pinnatifida Bge. : 최유진

다국어 초록 (Multilingual Abstract)

Cratagus pinnatifida Bunge (Hawthorn) is widely distributed in the northeast region South Korea. It is used as a medicinal plant to improve digestion, remove retention of food, promote blood circulation and resolve blood stasis both in traditional and folk medicine. The monoamine substrates for monoamine oxidase include physiologically and pathologically important monoamine neurotransmitters, which play a central role in the neurological disorder. The study is examined the inhibitory activities against monoamine oxidase A and B of C. pinnatifida fruits using in vitro methods. The 80% methanol extracts from the fruits of C. pinnatifida fractionated successinely with solvent. Among the fractions, ethyl acetate fraction exhibited the most potent activities toward MAO-A (0.13 mg/ml) and MAO-B (0.21 mg/ml). Bioactive compounds were isolated from ethyl acetate fraction of C. pinnatifida with MAO inhibitory activities as guide assays and the chemical structures of isolated active compounds were identified through NMR/FT-IR (Nuclear magnetic resonance/ Fourier transform infrared spectroscopy). Thus compounds name is compound 1: {[(1-ethoxy-5-methoxy-1.5-dioxopentan-3-yl) amino] methoxy} acetic acid and compound 2: 4-amino-6-methoxy hept-6-enoic acid. IC50 of compound 1 were 0.034 mg/ml, 0.068 mg/m by MAO-A and MAO-B respectively. IC50 of compound 2 were 0.001 mg/ml, 0.025 mg/ml by MAO-A and MAO-B respectiveiy. Compound 2 showed more potent activity than compound 1. The separated materials from fruit of C. pinnatifida Bunge is possible candidate for mental disease of natural materials.

목차 (Table of Contents)

• 1 INTRODUCTION
• 2 LITERATURE REVIEW
• 2.1 Crataegus pinnatifida Bunge
• 2.1.1 Biological activities of Crataegus pinnatifida Bunge
• 2.1.2 Separate components of Crataegus pinnatifida Bunge
• 2.2 Monoamine oxidase 7
• 2.2.1 The Origin and structure of monoamine oxidase 7
• 2.2.2 The mechanism of monoamine oxidase 11
• 2.2.3 The studies about monoamine oxidase inhibitors 14
• 3 MATERIALS AND METHODS 19
• 3.1 Exprimental materials 19
• 3.2 Methods 20
• 3.2.1 Extraction and separation 20
• 3.2.2 Isolation and purification 21
• 3.2.3 Procedures of enzyme assay 22
• 3.3 Spectral data 24
• 3.3.1 Compound 1 24
• 3.3.2 Compound 2 29
• 4 RESULTS AND DISCUSSION 34
• 4.1 Monoamine oxidase inhibitory activity
• 4.1.1 Extract 34
• 4.1.2 Solevent graduation 37
• 4.1.3 Isolated compounds 42
• 4.2 Identification of separated materials 47
• 4.2.1 Compound 1 47
• 4.2.2 Compound 2 50
• 5 CONCLUSIONS 53
• BIBLIOGRAPHY 55
• ABSTRACT (in Korean) 62