Amyloid-like properties of a synthetic peptide corresponding to the carboxy terminus of beta-amyloid protein precursor.
Amyloid-like properties of a synthetic peptide corresponding to the carboxy terminus of beta-amyloid protein precursor.
复制标题
与 β-淀粉样蛋白前体的羧基末端相对应的合成肽的淀粉样蛋白样特性。
DOI：
10.1016/0003-9861(92)90068-8
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发表时间：
1992
影响因子：
3.9
通讯作者：
Kirschner,DA
中科院分区：
文献类型：
--
作者：
Caputo,CB;Fraser,PE;Sobel,IE;Kirschner,DA
发现一种合成肽（其序列对应于β-淀粉样蛋白前体（APP）羧基端20个氨基酸）在体外可形成纤维蛋白。这些纤维在用刚果红染色时在偏振光下显示双折射，当与硫磺素S结合时显示荧光，对蛋白酶具有抗性，并且具有交叉β构象。相比之下，具有来自APP胞内结构域的其他序列的肽和对应于该整个结构域的肽没有表现出β-淀粉样蛋白的全部性质。这些结果表明，来自β-淀粉样蛋白前体的C-末端的片段可以结合到神经元内成对的螺旋丝，并解释了其淀粉样蛋白的一些性质。
A synthetic peptide whose sequence corresponds to the 20 carboxy-terminal amino acids of β-amyloid protein precursor (APP) was found to form fibrilsin vitro. These fibrils showed birefringence in polarized light when stained with Congo red, fluoresced when bound with thioflavin S, were resistant to proteases, and had a crossβ conformation. By contrast, peptides with other sequences from the intracellular domain of APP and a peptide corresponding to this entire domain did not exhibit the full range of β-amyloid properties. These results suggest that a fragment from the C-terminus of the β-amyloid protein precursor could bind to intraneuronal paired helical filaments and account for some of its amyloid-like properties.