β-淀粉样蛋白基元序列寡聚化及纤维化的功能研究

发布时间：2018-04-23 05:30

本文选题：β-淀粉样蛋白 + 删节肽段　；参考：《重庆师范大学学报(自然科学版)》2017年01期

【摘要】：【目的】β-淀粉样蛋白形成的寡聚体是引起阿尔茨海默症(Alzheimer disease,AD)发病的主要原因之一,研究β-淀粉样蛋白各段序列在寡聚和纤维化过程中的作用,以便更好地阐明该蛋白的寡聚机制和毒性作用。【方法】以C-端及N-端删节的6种β-淀粉样肽段作为研究对象,通过硫磺素T荧光检测、Tris-Tricine电泳、透射电镜等方法定性定量分析这些肽段的寡聚化和纤维化能力。【结果】1)氨基酸37~42具有增强Aβ寡聚化和纤维化的功能;2)氨基酸18~36对于寡聚和纤维化很重要,但不能缺少N-端的参与;3)Aβ1-17参与β-淀粉样蛋白长纤维的形成。【结论】β-淀粉样蛋白各段氨基酸序列对该蛋白寡聚和纤维化所贡献的不同作用,这对于β-淀粉样蛋白毒性机制的研究起到一定的帮助作用。
[Abstract]:[objective] to study the role of 尾 -amyloid protein in the process of oligomerization and fibrosis, which is one of the main causes of Alzheimer disease (AD) caused by 尾 -amyloid protein (尾 -amyloid) oligodeoxynucleotides (尾 -amyloid). In order to better elucidate the oligomerization mechanism and toxicity of the protein. [methods] six 尾 -amyloid peptides with C-terminal and N-terminal deletions were used as research objects, and Tris-Tricine electrophoresis was detected by sulfur T fluorescence. Transmission electron microscopy and other methods were used to qualitatively analyze the oligomerization and fibrosis ability of these peptide segments. [results] 1) Amino acid 37N42 has the ability to enhance the function of A 尾 oligomerization and fibrosis) Amino acid 18N36 is very important for oligomerization and fibrosis. But N- terminus can not participate in the formation of 尾 -amyloid long fiber. [conclusion] the amino acid sequence of 尾 -amyloid protein plays a different role in the oligomerization and fibrosis of 尾 -amyloid protein. It is helpful to the study of 尾-amyloid protein toxicity mechanism.
【作者单位】：西藏民族大学基础医学院高原环境与疾病相关基因研究实验室;
【基金】：西藏自治区自然科学基金(No.12KJZRZMY02,2015zr-13-12)
【分类号】：R749.16

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