Inhibition of toxic metal-alpha synuclein interactions by human serum albumin

KM Pomier, R Ahmed, J Huang, G Melacini - Chemical Science, 2024 - pubs.rsc.org
Human serum albumin (HSA), the most abundant protein in plasma and cerebrospinal fluid,
not only serves as a crucial carrier of various exogenous and endogenous ligands but also …

Interaction of α-synuclein with divalent metal ions reveals key differences: A link between structure, binding specificity and fibrillation enhancement

A Binolfi, RM Rasia, CW Bertoncini… - Journal of the …, 2006 - ACS Publications
The aggregation of α-synuclein (AS) is characteristic of Parkinson's disease and other
neurodegenerative synucleinopathies. Interactions with metal ions affect dramatically the …

Metal interactions of α-synuclein probed by NMR amide-proton exchange

M Gonzalez-Garcia, G Fusco, A De Simone - Frontiers in Chemistry, 2023 - frontiersin.org
The aberrant aggregation of α-synuclein (αS), a disordered protein primarily expressed in
neuronal cells, is strongly associated with the underlying mechanisms of Parkinson's …

Copper (I)-α-synuclein interaction: structural description of two independent and competing metal binding sites

F Camponeschi, D Valensin, I Tessari… - Inorganic …, 2013 - ACS Publications
The aggregation of α-synuclein (αS) is a critical step in the etiology of Parkinson's disease.
Metal ions such as copper and iron have been shown to bind αS, enhancing its fibrillation …

Differential effects of Cu2+ and Fe3+ ions on in vitro amyloid formation of biologically-relevant α-synuclein variants

E Lorentzon, R Kumar, I Horvath, P Wittung-Stafshede - Biometals, 2020 - Springer
Alterations in metal ion homeostasis appear coupled to neurodegenerative disorders but
mechanisms are unknown. Amyloid formation of the protein α-synuclein in brain cells is a …

[HTML][HTML] Understanding the effect of the membrane-mimetic micelles on the interplay between α-synuclein and Cu (II)/Cu (I) cations

AB Uceda, R Ramis, K Pauwels, M Adrover… - Journal of Inorganic …, 2023 - Elsevier
Abstract α-Synuclein (αS) is a presynaptic protein whose aggregates are considered as a
hallmark of Parkinson's disease (PD). Although its physiological function is still under …

Site-specific interactions of Cu (II) with α and β-synuclein: Bridging the molecular gap between metal binding and aggregation

A Binolfi, GR Lamberto, R Duran… - Journal of the …, 2008 - ACS Publications
The aggregation of α-synuclein (AS) is a critical step in the etiology of Parkinson's disease
(PD) and other neurodegenerative synucleinopathies. Protein− metal interactions play a …

Copper2+ Binding to α-Synuclein. Histidine50 Can Form a Ternary Complex with Cu2+ at the N-Terminus but Not a Macrochelate

Y Tian, HF Stanyon, JD Barritt, U Mayet… - Inorganic …, 2019 - ACS Publications
α-Synuclein (αSyn) forms amyloid fibrils in the neurons of Parkinson's disease (PD) patients'.
Despite a role for Cu2+ in accelerating αSyn fibril formation, coupled with reports of copper …

Effects of the toxic metals arsenite and cadmium on α-synuclein aggregation in vitro and in cells

E Lorentzon, I Horvath, R Kumar, JI Rodrigues… - International journal of …, 2021 - mdpi.com
Exposure to heavy metals, including arsenic and cadmium, is associated with
neurodegenerative disorders such as Parkinson's disease. However, the mechanistic details …

[HTML][HTML] Zinc ions prevent α-synuclein aggregation by enhancing chaperone function of human serum albumin

S Al-Harthi, V Kharchenko, P Mandal… - International Journal of …, 2022 - Elsevier
Metal ions present in cellular microenvironment have been implicated as drivers of
aggregation of amyloid forming proteins. Zinc (Zn 2+) ions have been reported to directly …