Metal Binding of Alzheimer's Amyloid-β and Its Effect on Peptide Self-Assembly
A Abelein - Accounts of Chemical Research, 2023 - ACS Publications
Conspectus Metal ions have been identified as key factors modulating the aggregation of
amyloid-β peptide (Aβ) implicated in Alzheimer's disease (AD). The presence of elevated …
amyloid-β peptide (Aβ) implicated in Alzheimer's disease (AD). The presence of elevated …
Advances of metallodrug-amyloid β aggregation inhibitors for therapeutic intervention in neurodegenerative diseases: Evaluation of their mechanistic insights and …
Metal ions play a key role in aggregation of amyloid β protein by interfering with their proper
folding, altering protein homeostasis and cell viability, and ultimately leading to …
folding, altering protein homeostasis and cell viability, and ultimately leading to …
Structural dynamics of amyloid-β protofibrils and actions of anti-amyloid-β antibodies as observed by high-speed atomic force microscopy
T Watanabe-Nakayama, M Tsuji, K Umeda… - Nano Letters, 2023 - ACS Publications
Amyloid-β (Aβ) aggregation intermediates, including oligomers and protofibrils (PFs), have
attracted attention as neurotoxic aggregates in Alzheimer's disease. However, due to the …
attracted attention as neurotoxic aggregates in Alzheimer's disease. However, due to the …
NMR studies of amyloid interactions
DA Middleton - Progress in Nuclear Magnetic Resonance …, 2024 - Elsevier
Amyloid fibrils are insoluble, fibrous nanostructures that accumulate extracellularly in
biological tissue during the progression of several human disorders, including Alzheimer's …
biological tissue during the progression of several human disorders, including Alzheimer's …
Paramagnetic NMR to study iron sulfur proteins: 13C detected experiments illuminate the vicinity of the metal center
The robustness of NMR coherence transfer in proximity of a paramagnetic center depends
on the relaxation properties of the nuclei involved. In the case of Iron-Sulfur Proteins …
on the relaxation properties of the nuclei involved. In the case of Iron-Sulfur Proteins …
Copper trafficking system in cells: insights into coordination chemistry and toxicity
J Han - Dalton Transactions, 2023 - pubs.rsc.org
Transition metal ions, such as copper, are indispensable components in the biological
system. Copper ions which primarily exist in two major oxidation states Cu (I) and Cu (II) play …
system. Copper ions which primarily exist in two major oxidation states Cu (I) and Cu (II) play …
Smart Molecular Imaging and Theranostic Probes by Enzymatic Molecular In Situ Self-Assembly
X Wen, C Zhang, Y Tian, Y Miao, S Liu, JJ Xu, D Ye… - JACS Au, 2024 - ACS Publications
Enzymatic molecular in situ self-assembly (E-MISA) that enables the synthesis of high-order
nanostructures from synthetic small molecules inside a living subject has emerged as a …
nanostructures from synthetic small molecules inside a living subject has emerged as a …
Paramagnetic nuclear magnetic resonance: The Toolkit
Nuclear Magnetic Resonance (NMR) spectroscopy is the ideal tool to address the structure,
reactivity and dynamics of both inorganic and biological substances. The knowledge of …
reactivity and dynamics of both inorganic and biological substances. The knowledge of …
Chasing the Elusive “In‐Between” State of the Copper‐Amyloid β Complex by X‐ray Absorption through Partial Thermal Relaxation after Photoreduction
The redox activity of Cu ions bound to the amyloid‐β (Aβ) peptide is implicated as a source
of oxidative stress in the context of Alzheimer's disease. In order to explain the efficient redox …
of oxidative stress in the context of Alzheimer's disease. In order to explain the efficient redox …
Transition Metal Ion FRET-Based Probe to Study Cu (II)-Mediated Amyloid-β Ligand Binding
Recent therapeutic strategies suggest that small peptides can act as aggregation inhibitors
of monomeric amyloid-β (Αβ) by inducing structural rearrangements upon complexation …
of monomeric amyloid-β (Αβ) by inducing structural rearrangements upon complexation …