원문정보
초록
영어
Recent evidences suggest that Alzheimer's β-peptide (Aβ) aggregation and the toxicity in Alzheimer's disease (AD) are caused by abnormal interactions with metal ions, especially Zn2+, Cu2+, and Fe3+.1 While many studies had focused on the interaction of Aβ with single metal ion, such studies involving 'multiple' metal ions were hardly explored so far. Here, in order to
explore the nature of co-deposition of different metals, two or more metal ions along with Aβ were incubated over a solid surface with immobilized Aβ 42 oligomers. Our results indicated that the co-incubation of Cu2+, Zn2+ and Fe3+ significantly altered the morphology of aggregates. While the presence of Fe3+ alone resulted in the accelerated fibrillation of Aβ42, co-incubation of
Fe3+ with Cu2+ or Zn2+ resulted in formation of amorphous non-fibrillar deposits. In addition, sequential addition of Zn2+ or Cu2+ on fibrillar aggregates formed by Fe3+ demonstrated that Zn2+ and Cu2+ could possibly change the conformation of the aggregates induced by Fe3+. Our findings elucidate the outcome of co-existence of multiple metal ions through their interactions with Aβ peptides or its aggregates.