Screening of a Fraction with Higher Amyloid β Aggregation Inhibitory Activity from a Library Containing 210 Mushroom Extracts Using a Microliter-Scale High-Throughput Screening System with Quantum Dot Imaging
Alzheimer’s disease (AD) is a highly prevalent neurodegenerative disease hallmarked by amyloid plaques and neurofibrillary tangles. Amyloid plaques are formed by the amyloid β (Aβ) aggregation, so substances that inhibit this aggregation are useful for preventing and treating AD. Mushrooms are widel...
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2024-11-01
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| author | Gegentuya Huanood Mahadeva M. M. Swamy Rina Sasaki Keiya Shimamori Masahiro Kuragano Enkhmaa Enkhbat Yoshiko Suga Masaki Anetai Kenji Monde Kiyotaka Tokuraku |
| author_facet | Gegentuya Huanood Mahadeva M. M. Swamy Rina Sasaki Keiya Shimamori Masahiro Kuragano Enkhmaa Enkhbat Yoshiko Suga Masaki Anetai Kenji Monde Kiyotaka Tokuraku |
| author_sort | Gegentuya Huanood |
| collection | DOAJ |
| description | Alzheimer’s disease (AD) is a highly prevalent neurodegenerative disease hallmarked by amyloid plaques and neurofibrillary tangles. Amyloid plaques are formed by the amyloid β (Aβ) aggregation, so substances that inhibit this aggregation are useful for preventing and treating AD. Mushrooms are widely used medicinal fungi with high edible and nutritional value. Mushrooms have a variety of biologically active ingredients, and studies have shown that they have certain effects in anti-bacterial, anti-oxidation, anti-inflammatory, anti-tumor, and immune regulation. Previously, we developed a microliter-scale high-throughput screening (MSHTS) system using quantum dot (QD) nanoprobes to screen Aβ aggregation inhibitors. In this study, we appraised the Aβ aggregation inhibitory activity of 210 natural mushrooms from Hokkaido (Japan) and found 11 samples with high activity. We then selected <i>Elfvingia applanata</i> and <i>Fuscoporia obliqua</i> for extraction and purification as these samples were able to suppress Aβ-induced neurocytotoxicity and were readily available in large quantities. We found that the ethyl acetate (EtOAc) extract of <i>E. applanata</i> has high Aβ aggregation inhibitory activity, so we performed silica gel column chromatography fractionation and found that fraction 5 (f5) of the EtOAc extract displayed the highest Aβ aggregation inhibitory activity among all mushroom samples. The half-maximal effective concentration (EC<sub>50</sub>) value was 2.30 µg/mL, higher than the EC<sub>50</sub> of 10.7 µg/mL for rosmarinic acid, a well-known Aβ aggregation inhibitor. This inhibitory activity decreased with further purification, suggesting that some compounds act synergistically. The f5 fraction also inhibited the deposition of Aβ aggregates on the cell surface of human neuroblastoma SH-SY5Y cells. Our expectation is that f5, with additional tests, may eventually prove to be an inhibitor for the prevention of AD. |
| format | Article |
| id | doaj-art-2e38df9ba9ed49b799c51a2ea7ffb66c |
| institution | Kabale University |
| issn | 2304-8158 |
| language | English |
| publishDate | 2024-11-01 |
| publisher | MDPI AG |
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| series | Foods |
| spelling | doaj-art-2e38df9ba9ed49b799c51a2ea7ffb66c2024-12-13T16:26:28ZengMDPI AGFoods2304-81582024-11-011323374010.3390/foods13233740Screening of a Fraction with Higher Amyloid β Aggregation Inhibitory Activity from a Library Containing 210 Mushroom Extracts Using a Microliter-Scale High-Throughput Screening System with Quantum Dot ImagingGegentuya Huanood0Mahadeva M. M. Swamy1Rina Sasaki2Keiya Shimamori3Masahiro Kuragano4Enkhmaa Enkhbat5Yoshiko Suga6Masaki Anetai7Kenji Monde8Kiyotaka Tokuraku9Graduate School of Engineering, Muroran Institute of Technology, Muroran 050-8585, JapanFaculty of Advanced Life Science, Hokkaido University, Sapporo 001-0021, JapanGraduate School of Engineering, Muroran Institute of Technology, Muroran 050-8585, JapanGraduate School of Engineering, Muroran Institute of Technology, Muroran 050-8585, JapanGraduate School of Engineering, Muroran Institute of Technology, Muroran 050-8585, JapanFaculty of Advanced Life Science, Hokkaido University, Sapporo 001-0021, JapanFaculty of Advanced Life Science, Hokkaido University, Sapporo 001-0021, JapanFaculty of Advanced Life Science, Hokkaido University, Sapporo 001-0021, JapanFaculty of Advanced Life Science, Hokkaido University, Sapporo 001-0021, JapanGraduate School of Engineering, Muroran Institute of Technology, Muroran 050-8585, JapanAlzheimer’s disease (AD) is a highly prevalent neurodegenerative disease hallmarked by amyloid plaques and neurofibrillary tangles. Amyloid plaques are formed by the amyloid β (Aβ) aggregation, so substances that inhibit this aggregation are useful for preventing and treating AD. Mushrooms are widely used medicinal fungi with high edible and nutritional value. Mushrooms have a variety of biologically active ingredients, and studies have shown that they have certain effects in anti-bacterial, anti-oxidation, anti-inflammatory, anti-tumor, and immune regulation. Previously, we developed a microliter-scale high-throughput screening (MSHTS) system using quantum dot (QD) nanoprobes to screen Aβ aggregation inhibitors. In this study, we appraised the Aβ aggregation inhibitory activity of 210 natural mushrooms from Hokkaido (Japan) and found 11 samples with high activity. We then selected <i>Elfvingia applanata</i> and <i>Fuscoporia obliqua</i> for extraction and purification as these samples were able to suppress Aβ-induced neurocytotoxicity and were readily available in large quantities. We found that the ethyl acetate (EtOAc) extract of <i>E. applanata</i> has high Aβ aggregation inhibitory activity, so we performed silica gel column chromatography fractionation and found that fraction 5 (f5) of the EtOAc extract displayed the highest Aβ aggregation inhibitory activity among all mushroom samples. The half-maximal effective concentration (EC<sub>50</sub>) value was 2.30 µg/mL, higher than the EC<sub>50</sub> of 10.7 µg/mL for rosmarinic acid, a well-known Aβ aggregation inhibitor. This inhibitory activity decreased with further purification, suggesting that some compounds act synergistically. The f5 fraction also inhibited the deposition of Aβ aggregates on the cell surface of human neuroblastoma SH-SY5Y cells. Our expectation is that f5, with additional tests, may eventually prove to be an inhibitor for the prevention of AD.https://www.mdpi.com/2304-8158/13/23/3740mushroomquantum dot nanoprobesamyloid βAlzheimer’s diseaseinhibitornatural compounds |
| spellingShingle | Gegentuya Huanood Mahadeva M. M. Swamy Rina Sasaki Keiya Shimamori Masahiro Kuragano Enkhmaa Enkhbat Yoshiko Suga Masaki Anetai Kenji Monde Kiyotaka Tokuraku Screening of a Fraction with Higher Amyloid β Aggregation Inhibitory Activity from a Library Containing 210 Mushroom Extracts Using a Microliter-Scale High-Throughput Screening System with Quantum Dot Imaging Foods mushroom quantum dot nanoprobes amyloid β Alzheimer’s disease inhibitor natural compounds |
| title | Screening of a Fraction with Higher Amyloid β Aggregation Inhibitory Activity from a Library Containing 210 Mushroom Extracts Using a Microliter-Scale High-Throughput Screening System with Quantum Dot Imaging |
| title_full | Screening of a Fraction with Higher Amyloid β Aggregation Inhibitory Activity from a Library Containing 210 Mushroom Extracts Using a Microliter-Scale High-Throughput Screening System with Quantum Dot Imaging |
| title_fullStr | Screening of a Fraction with Higher Amyloid β Aggregation Inhibitory Activity from a Library Containing 210 Mushroom Extracts Using a Microliter-Scale High-Throughput Screening System with Quantum Dot Imaging |
| title_full_unstemmed | Screening of a Fraction with Higher Amyloid β Aggregation Inhibitory Activity from a Library Containing 210 Mushroom Extracts Using a Microliter-Scale High-Throughput Screening System with Quantum Dot Imaging |
| title_short | Screening of a Fraction with Higher Amyloid β Aggregation Inhibitory Activity from a Library Containing 210 Mushroom Extracts Using a Microliter-Scale High-Throughput Screening System with Quantum Dot Imaging |
| title_sort | screening of a fraction with higher amyloid β aggregation inhibitory activity from a library containing 210 mushroom extracts using a microliter scale high throughput screening system with quantum dot imaging |
| topic | mushroom quantum dot nanoprobes amyloid β Alzheimer’s disease inhibitor natural compounds |
| url | https://www.mdpi.com/2304-8158/13/23/3740 |
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