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没食子酸与猪血红蛋白相互作用:对血红蛋白氧化还原状态和结构的影响。

Interactions of Gallic Acid with Porcine Hemoglobin: Effect on the Redox State and Structure of Hemoglobin.

机构信息

College of Biomass Science and Engineering, Sichuan University, Chengdu 610065, P. R. China.

Department of Inspection, Chengdu Medical College, Chengdu 610101, P. R. China.

出版信息

J Agric Food Chem. 2021 Jan 13;69(1):397-403. doi: 10.1021/acs.jafc.0c06204. Epub 2020 Dec 22.

DOI:10.1021/acs.jafc.0c06204
PMID:33351608
Abstract

The effect of gallic acid (GA) on the redox state of hemoglobin (Hb) and the structural mechanism upon the Hb-GA interaction were investigated. Results indicated that GA exhibited antioxidant and pro-oxidant effects on Hb, which depended on its concentration and the redox state of Hb. The antioxidant capacity of GA contributed to the inhibition of free iron release from Hb. GA could bind to the central cavity of Hb and interacted with the heme moiety through direct hydrophobic contacts as indicated by docking analysis, but GA did not disrupt the heme structure. Conversely, GA increased the compactness of the Hb molecule and might narrow the crevice around the heme pocket, which contributed to the inhibition of Hb autoxidation and the free iron release. Results provided significant insights into the interaction of GA with redox-active Hb, which is beneficial to the application of GA in relative meat and blood products.

摘要

研究了没食子酸(GA)对血红蛋白(Hb)氧化还原状态的影响及其与 Hb 相互作用的结构机制。结果表明,GA 对 Hb 表现出抗氧化和促氧化作用,这取决于其浓度和 Hb 的氧化还原状态。GA 的抗氧化能力有助于抑制 Hb 中游离铁的释放。对接分析表明,GA 可以结合到 Hb 的中心腔,并通过直接的疏水性接触与血红素部分相互作用,但 GA 不会破坏血红素结构。相反,GA 增加了 Hb 分子的紧凑性,并可能缩小血红素口袋周围的缝隙,这有助于抑制 Hb 自氧化和游离铁的释放。研究结果为 GA 与氧化还原活性 Hb 的相互作用提供了重要的见解,这有利于 GA 在相关肉类和血液制品中的应用。

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