Advances in structures required of polyphenols for xanthine oxidase inhibition
Abstract Polyphenols have been used as natural medicaments for the management of hyperuricemia for a long history. They have been attracted many interests because of the little side effects in curing hyperuricemia, which is an important advantage over the antihyperuricemic drugs. In this review, the...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Wiley
2020-06-01
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| Series: | Food Frontiers |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/fft2.27 |
| _version_ | 1818669056462422016 |
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| author | Liangliang Liu Li Zhang Licheng Ren Yixi Xie |
| author_facet | Liangliang Liu Li Zhang Licheng Ren Yixi Xie |
| author_sort | Liangliang Liu |
| collection | DOAJ |
| description | Abstract Polyphenols have been used as natural medicaments for the management of hyperuricemia for a long history. They have been attracted many interests because of the little side effects in curing hyperuricemia, which is an important advantage over the antihyperuricemic drugs. In this review, the structure–activity relationships for polyphenols as xanthine oxidase (XO) inhibitors were discussed. It is concluded that the presence of hydroxyl groups, which influences the inhibitory effects, is closely related to whether the substitutions increase the steric hindrance or disturb the interaction of flavonoid with the catalytic site of XO, and the increased size of the molecule after glycosylation may increase the steric hindrance between flavonoid and XO, and consequently reducing the competitive inhibition behaviors. However, there is no obtained simple general rule that can comprehensively describe the effects of structural alteration on the inhibition activity because the results are varied among different subclasses of polyphenols. In addition, the inhibition mechanisms are mainly assumed as polyphenol binding to the active site of XO and hindering the entrance of xanthine or the discharge of uric acid and diffusion of O2− radical. |
| first_indexed | 2024-12-17T06:46:09Z |
| format | Article |
| id | doaj.art-a0efedce5d8d4e48a0c3c1bf2e01c347 |
| institution | Directory Open Access Journal |
| issn | 2643-8429 |
| language | English |
| last_indexed | 2024-12-17T06:46:09Z |
| publishDate | 2020-06-01 |
| publisher | Wiley |
| record_format | Article |
| series | Food Frontiers |
| spelling | doaj.art-a0efedce5d8d4e48a0c3c1bf2e01c3472022-12-21T21:59:44ZengWileyFood Frontiers2643-84292020-06-011215216710.1002/fft2.27Advances in structures required of polyphenols for xanthine oxidase inhibitionLiangliang Liu0Li Zhang1Licheng Ren2Yixi Xie3Institute of Bast Fiber Crops Chinese Academy of Agricultural Sciences Changsha 410205 ChinaCollege of Chemistry and Materials Engineering Huaihua University Huaihua 418000 ChinaInstitute of Bast Fiber Crops Chinese Academy of Agricultural Sciences Changsha 410205 ChinaInstitute of Bast Fiber Crops Chinese Academy of Agricultural Sciences Changsha 410205 ChinaAbstract Polyphenols have been used as natural medicaments for the management of hyperuricemia for a long history. They have been attracted many interests because of the little side effects in curing hyperuricemia, which is an important advantage over the antihyperuricemic drugs. In this review, the structure–activity relationships for polyphenols as xanthine oxidase (XO) inhibitors were discussed. It is concluded that the presence of hydroxyl groups, which influences the inhibitory effects, is closely related to whether the substitutions increase the steric hindrance or disturb the interaction of flavonoid with the catalytic site of XO, and the increased size of the molecule after glycosylation may increase the steric hindrance between flavonoid and XO, and consequently reducing the competitive inhibition behaviors. However, there is no obtained simple general rule that can comprehensively describe the effects of structural alteration on the inhibition activity because the results are varied among different subclasses of polyphenols. In addition, the inhibition mechanisms are mainly assumed as polyphenol binding to the active site of XO and hindering the entrance of xanthine or the discharge of uric acid and diffusion of O2− radical.https://doi.org/10.1002/fft2.27inhibitorsnatural productspolyphenolsstructurexanthine oxidase |
| spellingShingle | Liangliang Liu Li Zhang Licheng Ren Yixi Xie Advances in structures required of polyphenols for xanthine oxidase inhibition Food Frontiers inhibitors natural products polyphenols structure xanthine oxidase |
| title | Advances in structures required of polyphenols for xanthine oxidase inhibition |
| title_full | Advances in structures required of polyphenols for xanthine oxidase inhibition |
| title_fullStr | Advances in structures required of polyphenols for xanthine oxidase inhibition |
| title_full_unstemmed | Advances in structures required of polyphenols for xanthine oxidase inhibition |
| title_short | Advances in structures required of polyphenols for xanthine oxidase inhibition |
| title_sort | advances in structures required of polyphenols for xanthine oxidase inhibition |
| topic | inhibitors natural products polyphenols structure xanthine oxidase |
| url | https://doi.org/10.1002/fft2.27 |
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