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Metal-binding Ability of Peptides Originating from Prion Protein by a Column Switch HPLC

机译:柱开关HPLC源自朊病毒蛋白的肽的金属结合能力

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In the cause of the prion disease, Cu~(2+) is thought to be concerned in denaturation of prion protein from normal type to the anomaly. In this study, we test the binding abilities of nine synthetic peptides to various metal ions by a column switch HPLC system. One octarepeat region (OP-l.PHGGGWGQ) binds to only Ni~(2+) and Zn~(2+). Two (OP-2), three (OP-3) and four octarepeat regains (OP-4) bind to Cu~(2+), Ni~(2+), Zn~(2+) and Co~(2+). In addition, the other peptides tested here also bind mainly Cu~(2+). This indicates the prion protein possesses many Cu~(2+) binding site.
机译:在朊病毒疾病的原因中,Cu〜(2+)被认为涉及从正常类型到异常的朊病毒蛋白的变性。在该研究中,我们通过柱开关HPLC系统测试九个合成肽对各种金属离子的结合能力。一个八烯糖区(OP-L.PHGGGGWGQ)只结合Ni〜(2+)和Zn〜(2+)。两个(OP-2),三(OP-3)和四个八烯糖糖(OP-4)与Cu〜(2+),Ni〜(2+),Zn〜(2+)和Co〜(2+ )。此外,这里测试的其他肽也主要结合Cu〜(2+)。这表明朊病毒蛋白具有许多Cu〜(2+)结合位点。

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