Hornshaw M P, McDermott J R, Candy J M
MRC Neurochemical Pathology Unit, Newcastle General Hospital, Newcastle upon Tyne, United Kingdom.
Biochem Biophys Res Commun. 1995 Feb 15;207(2):621-9. doi: 10.1006/bbrc.1995.1233.
Mammalian prion protein (PrP) is a normal cellular protein (PrPc) which through post-translational modification produces the infectious prion protein (PrPsc). We have shown, using mass spectrometry, that synthetic peptides containing three or four copies of an octapeptide repeat sequence (PHGGGWGQ), found in a highly conserved N-terminal domain of PrP, preferentially bind copper over other metals. Peptides from the analogous region of chicken PrP, which contains an N-terminal repeat domain of the hexapeptide (NPGYPH), showed similar specificity for copper binding. In addition, gel filtration chromatography demonstrated concentration dependent binding of copper to the mammalian tetra repeat PrP peptide. These results suggest that PrP may be a copper binding protein in vivo.
哺乳动物朊病毒蛋白（PrP）是一种正常的细胞蛋白（PrPc），它通过翻译后修饰产生感染性朊病毒蛋白（PrPsc）。我们已经通过质谱分析表明，在PrP高度保守的N端结构域中发现的含有三个或四个八肽重复序列（PHGGGWGQ）的合成肽，与其他金属相比，对铜具有优先结合性。来自鸡PrP类似区域的肽，其含有六肽（NPGYPH）的N端重复结构域，对铜结合表现出类似的特异性。此外，凝胶过滤色谱法证明铜与哺乳动物四重复PrP肽的结合具有浓度依赖性。这些结果表明，PrP在体内可能是一种铜结合蛋白。
