| 崔宇博， 李瑞， 秦那日苏， 关心语， 包小兰.亚麻籽蛋白源巯基肽与铅离子螯合作用及其对
铅中毒小鼠肝脏、肾脏的保护作用[J].中国油脂,2026,51(4):.[CUI Yubo, LI Rui, QIN Narisu, GUAN Xinyu, BAO Xiaolan.Chelation of lead ions by flaxseed protein-derived sulfhydryl peptides and their protective effects on the liver and kidney in lead-poisoned mice[J].China Oils and Fats,2026,51(4):.] |
| 亚麻籽蛋白源巯基肽与铅离子螯合作用及其对
铅中毒小鼠肝脏、肾脏的保护作用 |
| Chelation of lead ions by flaxseed protein-derived sulfhydryl peptides and their protective effects on the liver and kidney in lead-poisoned mice |
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| DOI：10.19902/j.cnki.zgyz.1003-7969.250070 |
| 中文关键词: 亚麻籽蛋白 巯基肽 螯合作用 铅中毒 保护作用 |
| 英文关键词:flaxseed protein sulfhydryl peptides chelation lead poisoning protective effect |
| 基金项目:内蒙古自然科学基金（2023MS03017）；国家自然科学基金（32360553）；内蒙古教育厅一流学科专项（YLXKZX-NND-015）；内蒙古农业大学食品科学与工程学院科技项目（SPKJ202212） |
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| 中文摘要: |
| 旨在探究亚麻籽蛋白源巯基肽（FSP）对铅中毒小鼠肝脏、肾脏的保护作用，对FSP的巯基含量、铅螯合量以及一级结构进行分析，对FSP进行分子动力学模拟实验以分析FSP的作用机制，并通过动物实验考察FSP对铅中毒小鼠肝脏和肾脏指标的影响。结果表明：FSP的巯基含量和铅螯合量分别达到71.13 μmol/g和23.90 mg/g，分别是亚麻籽蛋白的8.24倍和3.73倍；FSP中鉴定出34种含有巯基的肽段，其中选取的有代表性的3种肽段的分子动力学模拟结果表明，FSP与铅螯合的关键位点为半胱氨酸的硫原子，甘氨酸、天冬氨酸、谷氨酸和脯氨酸上的氧原子及谷氨酰胺上的氧原子和氮原子，且铅与3种肽段的螯合作用相对稳定；动物实验结果表明，FSP可改善铅中毒小鼠的体质量、肝脏指数和肾脏指数异常，降低铅中毒小鼠血液、肝脏和肾脏中的铅含量，提高粪便中铅含量，缓解铅中毒小鼠肝脏、肾脏组织病理学异常改变，并逆转铅中毒小鼠血清中谷丙转氨酶、谷草转氨酶、尿酸、肌酐和尿素氮水平异常。综上，推测FSP通过与铅离子形成螯合物，促进小鼠体内铅随粪便排出，从而对小鼠肝脏、肾脏产生保护作用。 |
| 英文摘要: |
| To elucidate the protective effects of flaxseed protein-derived sulfhydryl peptides (FSP) on the liver and kidney in lead-poisoned mice, the sulfhydryl content, lead chelation capacity, and primary structure of FSP were analyzed. Molecular dynamics simulations were conducted to investigate the action mechanism of FSP, and animal experiments were performed to examine the effects of FSP on liver and kidney indicators in lead-poisoned mice. The results showed that the sulfhydryl content and lead chelation capacity of FSP reached 71.13 μmol/g and 23.90 mg/g, respectively, which were 8.24 times and 3.73 times of those of flaxseed protein. A total of 34 sulfhydryl-containing peptides were identified in FSP. Molecular dynamics simulations of three representative peptides revealed that the key binding sites of FSP for lead chelation were sulfur atom on cysteine, oxygen atom on glycine, aspartic acid, glutamic and proline, oxygen and nitrogen atoms on glutamine, and the chelation interactions between lead and peptides were relatively stable. Animal experiments demonstrated that FSP improved the abnormal body weight, liver coefficient, and kidney coefficient of lead-poisoned mice, reduced lead levels in the blood, liver, and kidney, while increasing lead excretion in feces, alleviated the abnormal histopathological changes of liver and kidney tissues in lead-poisoned mice, and reversed abnormal levels of alanine aminotransferase, aspartate aminotransferase, uric acid, creatinine, and urea nitrogen in the serum of lead-poisoned mice. In conclusion, it is hypothesized that FSP protects the liver and kidney of lead-poisoned mice by forming chelates with lead ions and promoting their excretion through feces. |
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