State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, Jiangsu, P. R. China.
School of Food Science and Technology, Jiangnan University, Wuxi 214122, Jiangsu, P. R. China.
J Agric Food Chem. 2022 Feb 23;70(7):2179-2186. doi: 10.1021/acs.jafc.1c05583. Epub 2022 Feb 11.
-(1-Deoxy-d-fructos-1-yl)-histidine (Fru-His), one of the Amadori compounds, widely presents in processed foods, and its potential functional activities have attracted extensive attention in recent years. In this work, the angiotensin-converting enzyme (ACE) inhibitory activity and mechanism of Fru-His were investigated. The IC value of Fru-His was 0.150 ± 0.019 mM, and there was no obvious degradation of Fru-His after digestion simulation, showing that Fru-His has good ACE inhibition and digestive stability. Fru-His was a competitive inhibitor according to the enzyme inhibition kinetic analysis. The interaction between ACE and Fru-His occurred spontaneously mainly through hydrogen bonding, and the process was accompanied by fluorescence quenching and the alteration of the secondary structure of ACE. The molecular docking data supported the above results. Fru-His was attached to ACE's S1 active pocket through hydrogen bonds and interacted with zinc ions in active sites. The present study demonstrates that food-derived Fru-His has the potential to relieve hypertension.
（1-脱氧-d-果糖基）组氨酸（Fru-His）是美拉德反应产物之一，广泛存在于加工食品中，其潜在的功能活性近年来引起了广泛关注。本研究探讨了 Fru-His 的血管紧张素转化酶（ACE）抑制活性及其作用机制。结果表明，Fru-His 的 IC 值为 0.150±0.019mM，且经消化模拟后未见 Fru-His 明显降解，表明 Fru-His 具有良好的 ACE 抑制作用和消化稳定性。酶抑制动力学分析表明 Fru-His 为竞争性抑制剂。Fru-His 与 ACE 之间的相互作用主要通过氢键自发发生，该过程伴随着荧光猝灭和 ACE 二级结构的改变。分子对接数据支持了上述结果。Fru-His 通过氢键与 ACE 的 S1 活性口袋结合，并与活性位点中的锌离子相互作用。本研究表明，来源于食物的 Fru-His 具有缓解高血压的潜力。
