槲皮素 omega-6 和 -9 酯对蘑菇酪氨酸酶活性和结构的评价：光谱和分子对接研究,Journal of Food Biochemistry

当前位置： X-MOL 学术 › J. Food Biochem. › 论文详情

Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)

槲皮素 omega-6 和 -9 酯对蘑菇酪氨酸酶活性和结构的评价：光谱和分子对接研究
Journal of Food Biochemistry ( IF 3.5 ) Pub Date : 2021-09-29 , DOI: 10.1111/jfbc.13953
Morteza Vaezi ₁

Affiliation

槲皮素是最普遍存在的膳食类黄酮之一，广泛分布于植物和植物来源的食物中，是一种有效的酪氨酸酶抑制剂。槲皮素脂肪酸酯可提高槲皮素亲脂性，从而对其药理活性产生积极影响。在本研究中，通过实验和分子对接技术研究了槲皮素-亚油酸（配体 A）和槲皮素-油酸（配体 B）的两种新型酯对蘑菇酪氨酸酶 (MT) 的结构和双酚酶活性的抑制作用。在底物 3,4-二羟基苯丙氨酸 (L-多巴) 存在下使用紫外-可见分光光度法进行的抑制动力学研究表明，两种酯均成功抑制酪氨酸酶的活性并减少多巴醌的形成。结果表明配体与MT的结合诱导了酶的重排和构象变化。这些相互作用的热力学参数（K _a , ∆ G °, ∆ H ° 和 ∆ S °) 在 pH = 6.8 和 298 和 310 K 的温度下获得。分子对接研究进一步应用于计算结合能 (Δ G _bA = -21.84 kJ/mol , Δ G _bB = -20.92 kJ/mol), 抑制常数值 ( K _IA = 160 µM, K _IB = 220 µM) 和特殊的结合位点。可以推断配体作为潜在的酪氨酸酶抑制剂起作用，并且发现具有可视化结合模式的最佳可能相互作用条件是由配体 A 实现的，并表现出有效的酪氨酸酶抑制活性。这些发现可能有助于了解槲皮素脂肪酸酯对酪氨酸酶的抑制机制，并为区分酚类酪氨酸酶抑制剂提供一种便捷的筛选方法。

"点击查看英文标题和摘要"

Evaluation of quercetin omega-6 and -9 esters on activity and structure of mushroom tyrosinase: Spectroscopic and molecular docking studies

Quercetin is one of the most ubiquitous dietary flavonoids widely distributed in plants and foods of plant origin, and is a potent tyrosinase inhibitor. Quercetin fatty esters could lead to an improve in quercetin lipophilicity which could positively affect its pharmacological activity. In this study, the inhibitory effect of two novel esters of quercetin-linoleic acid (ligand A) and quercetin-oleic acid (ligand B) has been investigated on structure and diphenolase activity of mushroom tyrosinase (MT) by experimental and molecular docking techniques. The inhibitory kinetics study using UV-visible spectrophotometry in the presence of its substrate 3,4-dihydroxyphenylalanine (L-dopa), revealed that both esters successfully inhibit the activity of tyrosinase and reduce the formation of dopaquinone. Results showed that the binding of ligands to MT induced rearrangement and conformational changes of the enzyme. Thermodynamic parameters of these interactions (K_a, ∆G°, ∆H° and ∆S°) were obtained at pH = 6.8 and temperatures of 298 and 310 K. Molecular docking studies further was applied to calculation of binding energies (ΔG_bA = −21.84 kJ/mol, ΔG_bB = −20.92 kJ/mol), inhibition constant values (K_IA = 160 µM, K_IB = 220 µM) and the special binding site. It can be deduced that ligands act as a potential tyrosinase inhibitor and it was found that the best possible interaction condition with binding modes visualize was achieved by ligand A and exhibited the potent tyrosinase inhibitory activity. These findings may be helpful to understand the inhibition mechanism of quercetin fatty acids esters on tyrosinase and provide a convenient screening method to differentiate phenolic tyrosinase inhibitors.

更新日期：2021-11-07

点击分享查看原文

点击收藏

阅读更多本刊新发论文本刊介绍/投稿指南