Human serum albumin (HSA) is a major Cu carrier in human blood and cerebrospinal fluid. A assumption that bound to HSA the Cu(II) oxidation state; thus, interactions between have been intensely investigated for over four decades. has reported previously support reduction of Cu(I) state presence weak reductant, ascorbate; however, not explicitly investigated. Here, we characterize both apparent affinity using solution competition experiments coordination structure X-ray absorption...

Aβ4-42 is a major species of Aβ peptide in the brains both healthy individuals and those affected by Alzheimer's disease. It has recently been demonstrated to bind Cu(II) with an affinity approximately 3000 times higher than commonly studied Aβ1-42 Aβ1-40 peptides, which are implicated pathogenesis Metallothionein-3, protein considered orchestrate copper zinc metabolism brain provide antioxidant protection, was shown extract from when acting its native Zn7 MT-3 form. This reaction assumed...

The superior Cu(<sc>ii</sc>) affinity of human copper transporter 1 (hCtr1) drives acquisition from serum albumin (HSA).

Alzheimer’s disease (AD), one of the most common neurodegenerative diseases worldwide, is characterised by self-assembly amyloid-β peptides (Aβ) in senile plaques, which are also rich metal ions such as Cu and Zn. Here, we investigated influence Zn(II) on self- co-assembly Aβ1-40 N-terminally truncated Aβ4-40 peptides, two prevalent Aβ brain. The coordination site soluble model peptide Aβ4-16 was for first time through pH-dependent X-ray absorption spectroscopy nuclear magnetic resonance...

The human copper-binding protein metallothionein-3 (MT-3) can reduce Cu(II) to Cu(I) and form a polynuclear

Copper transfer from Cu(<sc>ii</sc>)amyloid-β_4–16 to human Zn₇-metallothionein-3 can be accelerated by glutamate and lowering the Zn-load of metallothionein-3 with EDTA.

Abstract Alzheimer's disease (AD) is one of the most common multifactorial diseases and characterized by a range abnormal molecular processes, such as accumulation extracellular plaques containing amyloid‐β (Aβ) peptides dyshomeostasis copper in brain. In this study, we have investigated effect Cu II on aggregation Aβ 1–40 4–40 , representing two prevalent families peptides, that is, full length N ‐truncated peptides. Both are similarly abundant healthy AD brains. For either studied...

The amyloid-β (Aβ) peptide is a cleavage product of the amyloid precursor protein and has been implicated as central player in Alzheimer's disease. N-terminal end Aβ variable, different proportions these variable-length peptides are present healthy individuals those with N-terminally truncated form starting at position 4 (Aβ4-x) His residue third amino acid (His6 using formal numbering). sequence Xaa-Xaa-His known an terminal copper nickel binding motif (ATCUN), which avidly binds Cu(II)....

Aβ4-42 is the major subspecies of Aβ peptides characterized by avid Cu(II) binding via ATCUN/NTS motif. It thought to be produced in vivo proteolytically neprilysin, but vitro experiments presence ions indicated preferable formation C-terminally truncated species including CuIIAβ4-16, CuIIAβ4-9, and also CuIIAβ12-16, all with nearly femtomolar affinities at neutral pH. Such small complexes may serve as shuttles for copper clearance from extracellular brain spaces, on condition they could...

N-Truncated Aβ4-42 displays a high binding affinity with CuII. A mechanistic scheme of the interactions between and CuII has been proposed using fluorescence approach. The timescales different conversion steps were determined. This kinetic mechanism indicates potential synaptic functions during neurotransmission.

Copper homeostasis is critical to the functioning of brain, and its breakdown linked with many brain diseases. also known interact negatively charged lipid, phosphatidylserine (PS), as well α-synuclein, an aggregation-prone protein enriched in synapse, which plays a role synaptic vesicle docking fusion. However, interplay between copper, PS α-synuclein not known. Herein, we report detailed predominantly kinetic study interactions among these three components pertinent copper...

Amyloid beta (Aβ) peptides are notorious for their involvement in Alzheimer's disease (AD), by virtue of propensity to aggregate form oligomers, fibrils, and eventually plaques the brain. Nevertheless, they appear be essential correct neurophysiology on synaptic level may have additional functions including antimicrobial activity, sealing blood–brain barrier, promotion recovery from brain injury, even tumor suppression. Aβ also avid copper chelators, coincidentally is significantly...

Abstract Aβ4‐42 is a major species of Aβ peptide in the brains both healthy individuals and those affected by Alzheimer's disease. It has recently been demonstrated to bind Cu II with an affinity approximately 3000 times higher than commonly studied Aβ1‐42 Aβ1‐40 peptides, which are implicated pathogenesis Metallothionein‐3, protein considered orchestrate copper zinc metabolism brain provide antioxidant protection, was shown extract from when acting its native Zn 7 MT‐3 form. This reaction...

Nickel is harmful to humans, being both carcinogenic and allergenic. However, the mechanisms of this toxicity are still unresolved. We propose that Ni(II) ions disintegrate proteins by hydrolysis peptide bonds preceding Ser/Thr-Xaa-His sequences. Such sequences occur in nuclear localization signals (NLSs) human phospholipid scramblase 1, Sam68-like mammalian protein 2, CLK3 kinase. performed spectroscopic experiments showing model nonapeptides derived from these NLSs bind at physiological...

Membrane binding and aggregation properties of alpha-synuclein are closely associated with Parkinson's disease a class related syndromes named as synucleinopathy. This study explored the potential SS-31 (Elamipretide), therapeutic tetrapeptide alternating cationic aromatic residues known mitochondrial inner membrane oxidative stress reduction, in modulating interaction lipid membranes mitigating impairment function induced by oligomers. It was demonstrated both fluorescence correlation...

His-Leu is a hydrolytic byproduct of angiotensin metabolism, whose concentration in the bloodstream could be at least micromolar. This encouraged us to investigate its Cu(II) binding properties and concomitant redox reactivity. The constants were derived from isothermal titration calorimetry potentiometry, while identities structures complexes obtained ultraviolet-visible, circular dichroism, room-temperature electronic paramagnetic resonance spectroscopies. Four types Cu(II)/His-Leu...