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近日，來(lái)自英國基爾大學(xué)的研究者通過(guò)研究揭示，銅不僅僅可以幫助個(gè)體的大腦抵御β-淀粉樣蛋白形成這折疊片，而且銅也直接參與了阿爾茲海默癥患者大腦中衰老斑的形成。

研究揭示，大腦中低水平的銅可以促進(jìn)某種特定機制的發(fā)生，這種機制就是在阿爾茲海默癥疾病中，β淀粉樣蛋白可以以衰老斑的形式存在。

目前研究者研究的重點(diǎn)就是調查是否大腦中的銅可以促使阿爾茲海默癥患者大腦中衰老斑的形成，此前研究中，研究者指出，銅的存在可以保護β淀粉樣蛋白免于聚集形成折疊片以及形成衰老斑，當然研究者希望通過(guò)后期的深入研究來(lái)闡明其中所發(fā)生的分子機理。

該項研究以“Copper prevents amyloid-β1-42 from forming amyloid fibrils under near-physiological conditions in vitro”為題刊登于國際著(zhù)名雜志雜志Nature的子刊Scientific Reports上。

The aggregation and deposition of amyloid-β(1–42) (Aβ42) in the brain is implicated in the aetiology of Alzheimer's disease (AD). While the mechanism underlying its deposition in vivo is unknown its precipitation in vitro is influenced by metal ions. For example, Aβ42 is known to bind copper, Cu(II), in vitro and binding results in aggregation of the peptide. The biophysical properties of Cu(II)-Aβ42 aggregates are of significant importance to their putative involvement in the amyloid cascade hypothesis of AD and are currently the subject of strong debate. In particular the question has been raised if sub- and super-stoichiometric concentrations of Cu(II) act in opposing ways in respectively accelerating and preventing amyloid fibril formation by Aβ42. Herein we have used fluorimetry and transmission electron microscopy to provide unequivocal evidence that under near-physiological conditions both sub- and super-stoichiometric concentrations of Cu(II) prevented the assembly of Aβ42 into ThT-positive β-sheet rich amyloid fibrils.