Intercommunication between metal ions and amyloidogenic peptides or proteins in protein misfolding disorders

Recent progress of small-molecule-based theranostic agents in Alzheimer's disease

“…The pathogenic roles of metal ions (e.g., copper, zinc, and iron) in AD have been widely recognized. 50,51 They can coordinate with Aβ and accelerate Aβ aggregation. In addition, copper and iron as redox active metals can also induce Aβ-mediated ROS production, thereby leading to oxidative stress.…”

Metal–BODIPY complexes: versatile photosensitizers for oxidizing amyloid-β peptides and modulating their aggregation profiles

“…[13][14][15][16][17][18][19][20] Amyloidogenic peptides and proteins exhibit a propensity to form β-sheet fibril structures through oligomeric conformations, and this aggregation process has been implicated in the pathogenesis of degenerative disorders. [21][22][23][24][25][26][27] Consequently, the ROS-mediated oxidative modification of amyloidogenic species by photosensitizers holds the potential to modulate their aggregation pathways, suggesting a prospective therapeutic approach (Fig. 1a).…”

Zn2+ Binding Increases Parallel Structure in the Aβ(16–22) Oligomer by Disrupting Salt Bridge in Antiparallel Structure

“…In vivo studies reported that Zn 2+ , Cu 2+ , and Fe 3+ are markedly enriched in Aβ plaques, ,, suggesting that these ions may act as seeding factors . In particular, under physiological conditions, there is ample evidence showing that the addition of Zn 2+ into Aβ peptides solution leads to the formation of neurotoxic nonfibrillar aggregates of Aβ − and simultaneously destabilizes the amyloid fibrils . Several studies have explored the binding site of Zn 2+ on Aβ aggregates.…”