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阿魏酸对糖基化终产物的抑制作用及其自由基清除能力:体外和分子对接研究。

Inhibition of advanced glycation end products by isoferulic acid and its free radical scavenging capacity: An in vitro and molecular docking study.

机构信息

Department of Biochemistry, JNMC, AMU, Aligarh, India.

Department of Biochemistry, F/O Life Sciences, AMU, Aligarh, India.

出版信息

Int J Biol Macromol. 2018 Oct 15;118(Pt B):1479-1487. doi: 10.1016/j.ijbiomac.2018.06.182. Epub 2018 Jun 30.

Abstract

Non-enzymatic glycation and Oxidation of some essential biological macromolecules are paramount in the pathogenesis of various diseases including diabetes and atherosclerosis. Hyperglycemia plays a key role in the pathological process of diabetic complications by progressive accumulation of advanced glycation end products (AGEs) in body tissues. Formation of AGEs as a result of protein glycation is followed by an increased free radical activity that additionally contributes towards the bio-macromolecular damage. The present study aimed to evaluate the free radical scavenging and antiglycation capacity of isoferulic acid (IFA). The free radical scavenging activity of IFA was measured using DPPH, FRAP, and metal chelating assays. IFA showed effective reducing power, free radical scavenging activity and metal chelation activity in concentration dependent manner. The antiglycation activity of IFA was studied using various spectroscopic techniques. The obtained results were validated with free amino, sulfhydryl group, carbonyl content and AGEs formation. Secondary structural alterations were monitored using circular dichroism, morphology of aggregates was analyzed using transmission electron microscopy. Molecular docking reveals the possible binding location of IFA with in the sub-domain IIA of human serum albumin (HSA).

摘要

非酶糖化和某些重要生物大分子的氧化在各种疾病的发病机制中至关重要,包括糖尿病和动脉粥样硬化。高血糖通过在体内组织中渐进性积累晚期糖基化终产物(AGEs),在糖尿病并发症的病理过程中发挥关键作用。蛋白质糖化导致 AGEs 的形成,随后自由基活性增加,这进一步导致生物大分子损伤。本研究旨在评估异阿魏酸(IFA)的自由基清除和抗糖化能力。使用 DPPH、FRAP 和金属螯合测定法测量 IFA 的自由基清除活性。IFA 表现出有效的还原能力、自由基清除活性和浓度依赖性金属螯合活性。使用各种光谱技术研究了 IFA 的抗糖化活性。用游离氨基、巯基、羰基含量和 AGEs 形成来验证获得的结果。使用圆二色性监测二级结构的变化,使用透射电子显微镜分析聚集体的形态。分子对接揭示了 IFA 与人血清白蛋白(HSA)亚域 IIA 内的可能结合位置。

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