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首页> 外文期刊>The FEBS journal >High affinity copper binding by stefin B (cystatin B) and its role in the inhibition of amyloid fibrillation
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High affinity copper binding by stefin B (cystatin B) and its role in the inhibition of amyloid fibrillation

机译：Stefin B（胱抑素B）与铜的高亲和力结合及其在抑制淀粉样蛋白原纤化中的作用

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We show that human stefin B, a protease inhibitor from the family of cystatins, is a copper binding protein, unlike stefin A. We have used isothermal titration calorimetry to directly monitor the binding event at pH 7 and pH 5. At pH 7 stefin B shows a picomolar affinity for copper but at pH 5 the affinity is in the nanomolar range. There is no difference in the affinity of copper between the wildtype stefin B (E31 isoform) and a variant (Y31 isoform), whereas the mutant (P79S), which is tetrameric, does not bind copper. The conformation of stefin B remains unaltered by copper binding. It is known that below pH 5 stefin B undergoes a conformational change and amyloid fibril formation. We show that copper binding inhibits the amyloid fibril formation and, to a lesser degree, the initial aggregation. Similarities to and differences from other copper binding amyloidogenic proteins are discussed.
机译：我们显示，人Stefin B（一种来自胱抑素家族的蛋白酶抑制剂）是铜结合蛋白，与Stefin A不同。我们已使用等温滴定热法直接监测pH 7和pH 5下的结合事件。在pH 7时Stefin B图1显示了对铜的皮摩尔亲和力，但是在pH 5下，亲和力在纳摩尔范围内。野生型Stefin B（E31亚型）和变体（Y31亚型）之间的铜亲和力没有差异，而四聚体的突变体（P79S）不结合铜。 Stefin B的构象保持不变与铜结合。已知在低于pH 5的条件下，stefin B发生构象变化和淀粉样原纤维形成。我们表明铜结合抑制淀粉样蛋白原纤维的形成，并在较小程度上抑制初始聚集。讨论了与其他铜结合淀粉样蛋白的相似之处和不同之处。

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