人工设计GAV-6短肽自组装形成淀粉样纤维的研究

发布时间：2018-03-16 23:10

本文选题：短肽　切入点：自组装　出处：《生物医学工程学杂志》2014年03期 　论文类型：期刊论文

【摘要】：淀粉样纤维是一类与人类疾病密切相关的蛋白异常聚集体,从一些核心短肽序列入手研究天然蛋白形成淀粉样纤维的分子机制是近年来的研究热点。本文设计了一个由甘氨酸(G)、丙氨酸(A)、缬氨酸(V)三种疏水性氨基酸构成的六肽GGAAVV(GAV-6),并研究其形成淀粉样纤维的能力。以原子力显微镜(AFM)和动态光散射(DLS)为手段的纳米结构表征发现,GAV-6能够在水溶液中自组装形成光滑不分叉的纳米纤维。通过刚果红染色/结合实验和硫磺素T结合实验,我们证实了这些纳米纤维具有典型的淀粉样纤维的特征。上述结果表明,人工设计的GAV-6短肽能够自组装形成淀粉样纤维,这可能为今后深入研究天然蛋白形成淀粉样纤维的机制提供一种简单的模式分子。
[Abstract]:Amyloid fibers are a class of abnormal protein aggregates closely related to human diseases. The molecular mechanism of the formation of amyloid fibers from natural proteins from some core short peptide sequences has been a hot topic in recent years. In this paper, a novel hydrophobic amino acid composed of three kinds of hydrophobic amino acids, glycine, alanine, and valine, was designed. The nanostructure characterization using AFM and DLSs showed that GAV-6 could self-assemble in aqueous solution to form smooth and non-branched nanofibers, which were characterized by atomic force microscopy (AFM) and dynamic light scattering (DLSs). PerCongo red staining / binding test and sulfur T binding test, We have confirmed that these nanofibers have the characteristics of typical amyloid fibers. These results show that the artificially designed GAV-6 short peptides can self-assemble to form amyloid fibers. This may provide a simple model molecule for the further study of the mechanism of the formation of amyloid fibers by natural proteins.
【作者单位】：四川大学华西医院卫生部移植工程与移植免疫重点实验室;四川大学华西医院再生医学研究中心;四川大学华西医院期刊社;
【基金】：国家自然科学基金资助项目(81000658,31100565,51003065)
【分类号】：R318.08

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