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首页> 外文期刊>Archives of Biochemistry and Biophysics >A beta 40 has a subtle effect on A beta 42 protofibril formation, but to a lesser degree than A beta 42 concentration in A beta 42/A beta 40 mixtures
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A beta 40 has a subtle effect on A beta 42 protofibril formation, but to a lesser degree than A beta 42 concentration in A beta 42/A beta 40 mixtures

机译：Beta 40对A beta 42的原纤维形成有微妙的影响，但程度要小于A beta 42 / A beta 40混合物中A beta 42的浓度

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Recent findings suggest that the senile plaques in Alzheimer's disease may contain soluble amyloid-beta peptide (A beta) fibril precursors along with insoluble fibrils. These soluble A beta species, including oligomers and protofibrils, have been well-studied in vitro and are formed via non-covalent self-assembly of A beta monomers. While both 40- and 42-residue forms of A beta are observed in the human body, the majority of the A beta aggregation work has been conducted on A beta 42 or A beta 40 separately, with relatively few investigations of mixtures. In order to study the effect of different combinations of A beta 40 and A beta 40 on protofibril formation, mixtures of either dry solid peptide, or purified A beta 40 and A beta 40 monomer solutions were mixed together and protofibril/monomer distributions were quantified. Increases in the A beta 42/A beta 40 ratio increased protofibril formation but the presence of A beta 40 in the mixed A beta solutions had a significant negative impact on protofibril formation compared to equivalent solutions of pure A beta 42. Protofibril size was less affected, but beta-sheet structure increased with protofibrils formed from higher A beta 42/A beta 40 ratio solutions. Direct measurement of A beta 42/A beta 40 ratios by C-terminal-selective ELISA found very little A beta 40 incorporated into protofibrils. The cumulative data emphasizes the critical importance of A beta 42, yet establishes A beta 40 as a regulator of A beta 42 aggregation. (C) 2016 Elsevier Inc. All rights reserved.
机译：最近的发现表明，阿尔茨海默氏病中的老年斑可能含有可溶性淀粉样β肽（A beta）原纤维前体以及不溶性原纤维。这些可溶性Aβ物质，包括低聚物和原纤维，已经在体外进行了充分研究，并通过Aβ单体的非共价自组装形成。虽然在人体中同时观察到40和42残基形式的A beta，但大多数A beta聚集工作是分别对A beta 42或A beta 40进行的，对混合物的研究相对较少。为了研究A beta 40和A beta 40的不同组合对原纤维形成的影响，将干燥的固体肽或纯化的A beta 40和A beta 40单体溶液的混合物混合在一起，并对原纤维/单体分布进行定量。 A beta 42 / A beta 40比值的增加会增加原纤维的形成，但是与纯A beta 42的同等溶液相比，混合的A beta溶液中A beta 40的存在对原纤维的形成具有显着的负面影响。原纤维的大小受到的影响较小，但随着更高的A beta 42 / A beta 40比溶液形成的原纤维，β-折叠结构增加了。通过C末端选择性ELISA直接测量A beta 42 / A beta 40的比率，发现掺入原纤维的Abeta 40很少。累积数据强调了A beta 42的至关重要性，但确立了A beta 40作为A beta 42聚集的调节剂。 （C）2016 Elsevier Inc.保留所有权利。

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