来自尼泊尔巴格马蒂省的六种当地植物的叶子提取物作为α-淀粉酶、脂肪酶、酪氨酸酶、弹性蛋白酶和胆碱酯酶的有效抑制剂

Q4 Pharmacology, Toxicology and Pharmaceutics Current Enzyme Inhibition Pub Date : 2020-11-04 DOI:10.2174/1573408016999200624150750
B. Pandey, S. Pradhan, K. Adhikari, Prayon Joshi, S. Malla
{"title":"来自尼泊尔巴格马蒂省的六种当地植物的叶子提取物作为α-淀粉酶、脂肪酶、酪氨酸酶、弹性蛋白酶和胆碱酯酶的有效抑制剂","authors":"B. Pandey, S. Pradhan, K. Adhikari, Prayon Joshi, S. Malla","doi":"10.2174/1573408016999200624150750","DOIUrl":null,"url":null,"abstract":"\n\nMedicinal plants and their products are gaining global popularity due to\ntheir several health benefits. However, the biological activities of the vast majority of medicinal plant\nspecies have not been explored yet. In this study, we evaluated the enzyme inhibitory potential of six\nmedicinal plant species involved in digestion, skin-related problems, and neurological problems.\n\n\n\nThe 80% methanol extracts of leaves of six locally available plants from the Bagmati province\nof Nepal were analyzed for their flavonoids content, phenolics content, antioxidant activity, and\nenzymes inhibitory potential. Antioxidant activity was analyzed by the DPPH assay. Alpha-amylase\ninhibition was carried out by the DNSA method. Lipase, tyrosinase, elastase, acetylcholinesterase,\nand butyrylcholinesterase inhibitions were analyzed by using p-NPB, L-DOPA, AAAPVN,\nacetylthiocholine, and butyrylthiocholine as a respective substrate.\n\n\n\nAmong the analyzed plants species, Artocarpus heterophyllus displayed highest α-amylase\n(IC50=6.28 ± 0.01 μg/mL), lipase (IC50= 475.14 ± 3.17 μg/mL), elastase (IC50= 72.75 ± 3.41 μg/mL)\nand acetylcholinesterase (IC50= 68.66 ± 1.71 μg/mL) inhibition, whereas, Actinidia deliciosa displayed\nhighest tyrosinase inhibition (IC50=139.87 ± 0.72 μg/mL) and butyrylcholinesterase inhibition\n(IC50= 18.32 ± 0.44 μg/mL). Furthermore, Jasminum humile showed no inhibitory tendencies against\nelastase and Lygodium japonicum showed no inhibition towards lipase and elastase at the given concentration\nrange.\n\n\n\nOur study revealed that A. deliciosa and A. heterophyllus are the potential source of α-\namylase, lipase, elastase, acetylcholinesterase, and butyrylcholinesterase inhibitors. Based on our\nfindings, we concluded that the analyzed plant species are of great scientific interest to the pharmaceutical,\ncosmetics, and food industries.\n","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2020-11-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"5","resultStr":"{\"title\":\"Extracts of Leaves of Six Locally Available Plants from Bagmati Province of Nepal as Potent Inhibitors of Alpha-amylase, Lipase, Tyrosinase, Elastase, and Cholinesterases\",\"authors\":\"B. Pandey, S. Pradhan, K. Adhikari, Prayon Joshi, S. Malla\",\"doi\":\"10.2174/1573408016999200624150750\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"\\n\\nMedicinal plants and their products are gaining global popularity due to\\ntheir several health benefits. However, the biological activities of the vast majority of medicinal plant\\nspecies have not been explored yet. In this study, we evaluated the enzyme inhibitory potential of six\\nmedicinal plant species involved in digestion, skin-related problems, and neurological problems.\\n\\n\\n\\nThe 80% methanol extracts of leaves of six locally available plants from the Bagmati province\\nof Nepal were analyzed for their flavonoids content, phenolics content, antioxidant activity, and\\nenzymes inhibitory potential. Antioxidant activity was analyzed by the DPPH assay. Alpha-amylase\\ninhibition was carried out by the DNSA method. Lipase, tyrosinase, elastase, acetylcholinesterase,\\nand butyrylcholinesterase inhibitions were analyzed by using p-NPB, L-DOPA, AAAPVN,\\nacetylthiocholine, and butyrylthiocholine as a respective substrate.\\n\\n\\n\\nAmong the analyzed plants species, Artocarpus heterophyllus displayed highest α-amylase\\n(IC50=6.28 ± 0.01 μg/mL), lipase (IC50= 475.14 ± 3.17 μg/mL), elastase (IC50= 72.75 ± 3.41 μg/mL)\\nand acetylcholinesterase (IC50= 68.66 ± 1.71 μg/mL) inhibition, whereas, Actinidia deliciosa displayed\\nhighest tyrosinase inhibition (IC50=139.87 ± 0.72 μg/mL) and butyrylcholinesterase inhibition\\n(IC50= 18.32 ± 0.44 μg/mL). Furthermore, Jasminum humile showed no inhibitory tendencies against\\nelastase and Lygodium japonicum showed no inhibition towards lipase and elastase at the given concentration\\nrange.\\n\\n\\n\\nOur study revealed that A. deliciosa and A. heterophyllus are the potential source of α-\\namylase, lipase, elastase, acetylcholinesterase, and butyrylcholinesterase inhibitors. Based on our\\nfindings, we concluded that the analyzed plant species are of great scientific interest to the pharmaceutical,\\ncosmetics, and food industries.\\n\",\"PeriodicalId\":35405,\"journal\":{\"name\":\"Current Enzyme Inhibition\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2020-11-04\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Current Enzyme Inhibition\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.2174/1573408016999200624150750\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"Pharmacology, Toxicology and Pharmaceutics\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Enzyme Inhibition","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2174/1573408016999200624150750","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"Pharmacology, Toxicology and Pharmaceutics","Score":null,"Total":0}
引用次数: 5

摘要

药用植物及其产品因其对健康的多种益处而在全球范围内越来越受欢迎。然而,绝大多数药用植物的生物活性尚未得到探索。在这项研究中,我们评估了六种涉及消化、皮肤相关问题和神经问题的药用植物的酶抑制潜力。对来自尼泊尔巴格马蒂省的六种当地植物的80%甲醇提取物的黄酮类化合物含量、酚类物质含量、抗氧化活性和酶抑制潜力进行了分析。DPPH法测定抗氧化活性。α淀粉酶的抑制作用采用DNSA法进行。使用p-NPB、L-DOPA、AAAPVN、乙酰硫胆碱和丁酰硫胆碱作为各自的底物来分析脂肪酶、酪氨酸酶、弹性蛋白酶、乙酰胆碱酯酶和丁酰胆碱酯酶的抑制作用。在所分析的植物物种中,异叶Artocarpus表现出最高的α-淀粉酶(IC50=6.28±0.01μg/mL)、脂肪酶(IC50=475.14±3.17μg/mL,美味猕猴桃对酪氨酸酶的抑制作用最高(IC50=139.87±0.72μg/mL),对丁酰胆碱酯酶的抑制作用最强(IC50=18.32±0.44μg/mL。此外,在一定浓度范围内,茉莉对弹性蛋白酶没有抑制作用,日本黄对脂肪酶和弹性蛋白酶也没有抑制作用。我们的研究表明,A.deliciosa和A.heterophylus是α-淀粉酶、脂肪酶、弹性蛋白酶、乙酰胆碱酯酶和丁酰胆碱酯酶抑制剂的潜在来源。根据我们的发现,我们得出结论,所分析的植物物种对制药、化妆品和食品行业具有重大的科学意义。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Extracts of Leaves of Six Locally Available Plants from Bagmati Province of Nepal as Potent Inhibitors of Alpha-amylase, Lipase, Tyrosinase, Elastase, and Cholinesterases
Medicinal plants and their products are gaining global popularity due to their several health benefits. However, the biological activities of the vast majority of medicinal plant species have not been explored yet. In this study, we evaluated the enzyme inhibitory potential of six medicinal plant species involved in digestion, skin-related problems, and neurological problems. The 80% methanol extracts of leaves of six locally available plants from the Bagmati province of Nepal were analyzed for their flavonoids content, phenolics content, antioxidant activity, and enzymes inhibitory potential. Antioxidant activity was analyzed by the DPPH assay. Alpha-amylase inhibition was carried out by the DNSA method. Lipase, tyrosinase, elastase, acetylcholinesterase, and butyrylcholinesterase inhibitions were analyzed by using p-NPB, L-DOPA, AAAPVN, acetylthiocholine, and butyrylthiocholine as a respective substrate. Among the analyzed plants species, Artocarpus heterophyllus displayed highest α-amylase (IC50=6.28 ± 0.01 μg/mL), lipase (IC50= 475.14 ± 3.17 μg/mL), elastase (IC50= 72.75 ± 3.41 μg/mL) and acetylcholinesterase (IC50= 68.66 ± 1.71 μg/mL) inhibition, whereas, Actinidia deliciosa displayed highest tyrosinase inhibition (IC50=139.87 ± 0.72 μg/mL) and butyrylcholinesterase inhibition (IC50= 18.32 ± 0.44 μg/mL). Furthermore, Jasminum humile showed no inhibitory tendencies against elastase and Lygodium japonicum showed no inhibition towards lipase and elastase at the given concentration range. Our study revealed that A. deliciosa and A. heterophyllus are the potential source of α- amylase, lipase, elastase, acetylcholinesterase, and butyrylcholinesterase inhibitors. Based on our findings, we concluded that the analyzed plant species are of great scientific interest to the pharmaceutical, cosmetics, and food industries.
求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Current Enzyme Inhibition
Current Enzyme Inhibition Pharmacology, Toxicology and Pharmaceutics-Drug Discovery
CiteScore
1.30
自引率
0.00%
发文量
30
期刊介绍: Current Enzyme Inhibition aims to publish all the latest and outstanding developments in enzyme inhibition studies with regards to the mechanisms of inhibitory processes of enzymes, recognition of active sites, and the discovery of agonists and antagonists, leading to the design and development of new drugs of significant therapeutic value. Each issue contains a series of timely, in-depth reviews written by leaders in the field, covering a range of enzymes that can be exploited for drug development. Current Enzyme Inhibition is an essential journal for every pharmaceutical and medicinal chemist who wishes to have up-to-date knowledge about each and every development in the study of enzyme inhibition.
期刊最新文献
Apocynaceae as a Potential Source for Acetylcholinesterase Inhibition in Symptomatic Regulation and Management of Alzheimer's Disease Inhibition of Perforin: A Potential Therapeutic Approach against Human Ailments Molecular Docking as a Method to Identify Prospective Compounds from Ocimum sanctum with Anti-Candidal Properties Design of Cyclobut-3-Ene-1,2 Dione Derivatives as Anti-tubercular Agents Enzyme Inhibition in Managing Cardiovascular Diseases
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1