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中国精品科技期刊2020
姜梦瑶,闫雨,关姣,等. 大分子拥挤环境下多酚结构类似物抑制人血清白蛋白聚集的研究[J]. 食品工业科技,2024,45(15):1−11. doi: 10.13386/j.issn1002-0306.2023100246.
引用本文: 姜梦瑶,闫雨,关姣,等. 大分子拥挤环境下多酚结构类似物抑制人血清白蛋白聚集的研究[J]. 食品工业科技,2024,45(15):1−11. doi: 10.13386/j.issn1002-0306.2023100246.
JIANG Mengyao, YAN Yu, GUAN Jiao, et al. Study on the Inhibition of Human Serum Albumin Aggregation by Polyphenols with Similar Structures in Macromolecular Crowding Environment[J]. Science and Technology of Food Industry, 2024, 45(15): 1−11. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2023100246.
Citation: JIANG Mengyao, YAN Yu, GUAN Jiao, et al. Study on the Inhibition of Human Serum Albumin Aggregation by Polyphenols with Similar Structures in Macromolecular Crowding Environment[J]. Science and Technology of Food Industry, 2024, 45(15): 1−11. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2023100246.

大分子拥挤环境下多酚结构类似物抑制人血清白蛋白聚集的研究

Study on the Inhibition of Human Serum Albumin Aggregation by Polyphenols with Similar Structures in Macromolecular Crowding Environment

  • 摘要: 为了揭示生理拥挤环境下巴西苏木素(Brazilin,Bra)、苏木素(Hematoxylin,Hto)和氧化苏木精(Hematein,Hte)抗蛋白质聚集能力,本文首先利用大分子拥挤试剂聚乙二醇构建了模拟拥挤环境,然后利用荧光光谱法、紫外-可见吸收光谱法、动态光散射法和原子力显微镜法研究了这三种结构类似的多酚类化合物对人血清白蛋白(HSA)聚集行为的抑制机制。结果表明,在拥挤环境中它们均能够维持HSA结构的稳定,减少形成的淀粉样纤维数量,缩短其长度,从而抑制蛋白质的聚集过程,且抑制能力依次为:Hto>Bra>Hte,此外,与体外稀溶液环境相比,拥挤试剂的存在会导致这三个抑制剂的抑制活性降低。总之,本研究表明Hto可作为潜在的蛋白质聚集抑制剂和功能性食品成分,用于淀粉样变性疾病的治疗干预。

     

    Abstract: To reveal the anti-protein aggregation ability of Brazilin (Bra), Hematoxylin (Hto) and Hematein (Hte) under physiological crowding environment, the macromolecular crowding reagent (polyethylene glycol) was used to construct a simulated crowding environment. Then the inhibition mechanisms of these three structurally similar polyphenol compounds on the aggregation behavior of human serum albumin (HSA) were investigated by fluorescence spectroscopy, UV-vis absorption spectroscopy, dynamic light scattering (DLS) and atomic force (AFM) microscope assay. The results showed that they could maintain the stability of the HSA structure, decrease the number of amyloid fibrils and shorten the length of aggregates in crowding environment. Therefore, they inhibited the aggregation process of HSA, and the sequence of the inhibition ability was in the order of Hto>Bra>Hte. Moreover, the presence of crowding reagents could lead to a decrease in the inhibitory activity of these three inhibitors compared to in vitro dilute solution. In conclusion, this study suggested that Hto could be used as a potential protein aggregation inhibitor and a functional food ingredient for the treatment and intervention of amyloid-related diseases.

     

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