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首页> 外文期刊>Biochemistry >The process-of amyloid-like fibril formation by methionine aminopeptidase from a hyperthermophile, Pyrococcus furiosus
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The process-of amyloid-like fibril formation by methionine aminopeptidase from a hyperthermophile, Pyrococcus furiosus

机译：由甲硫氨酸氨基肽酶从超嗜热嗜热偶联酶，Pyrococcus furoiosus的制备方法

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Amyloid is associated with serious diseases including Altzheimer's disease and senile-systemic amyloidosis due to misfolded proteins. In the course of study of the denaturation process of methionine aminopeptidase (MAP) from the hyperthermophile P. furiosus, we found that MAP forms amyloid-like fibrils, and we then investigated the mechanism of amyloid fibril formation. The kinetic experiments on denaturation monitored by CD at 222 nm indicated that MAP in the presence of 3.37 M GuHCl at pH 3.31 changed to a conformation containing a considerable content of beta-sheet structure after the destruction of the alpha-helical structure. MAP in this beta-rich conformation was highly associated, and its stability was remarkably high: the midpoint of the GuHCl denaturation curve was 4.82 M at pH 3.0, and a thermal transition was not observed up to 125 degrees C by calorimetry. The amyloid-like fibril formation of MAP was confirmed by Congo red staining with a typical peak at 542 nun in the difference spectrum, showing a cross-beta X-ray diffraction pattern with a clear sharp reflection at 4.7 Angstrom and a characteristic unbranched fibrillar appearance with a length of about 1000 Angstrom and a diameter of about 70 Angstrom in the electron micrographs. Present results indicate that the amyloid-like form of MAP appears just after the protein is almost completely denatured, and even highly stable proteins can also form amyloid-like conformation under conditions where the denatured state of the protein is abundantly populated. [References: 47]
机译：淀粉样蛋白与在包括Altzheimer的疾病和老年人的淀粉样蛋白病等严重疾病有关，由于错误折叠的蛋白质。在研究蛋氨酸氨基肽酶（MAP）的变性过程的过程中，我们发现MAP形成淀粉样蛋白样原纤维，然后研究了淀粉样蛋白原纤维形成的机制。在222nm处通过Cd监测的变性的动力学实验表明，在pH 3.31的3.37Mg GuhCl存在下，在破坏α-螺旋结构之后，在pH 3.31的存在下的含量变化为含有相当大的β-片状结构的构象。在这种β的构象中，地图具有高度相关的，其稳定性显着高：PH 3.0的GUHCL变性曲线的中点为4.82m，并且通过热量测定法未观察到热跃迁至125℃。通过在差异光谱中的542 nUN处的典型峰，在差异谱中具有典型峰，在差异谱中的典型峰，显示蛋白质的纤维状原纤维形成，显示出在4.7埃的尖锐βX射线衍射图案中，具有明显的尖锐反射和特征的非分支纤维状纤维状外观在电子显微照片中长度约1000埃和直径约70埃。目前的结果表明，在蛋白质几乎完全变性之后，且甚至高度稳定的蛋白质在蛋白质的变性状态大量填充的条件下也可以形成均匀稳定的蛋白质的淀粉样蛋白样形式。 [参考：47]

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