Rational design of photoactivatable metal complexes to target and modulate amyloid-β peptides

J Kwak, J Woo, S Park, MH Lim - Journal of Inorganic Biochemistry, 2023 - Elsevier
The accumulation of amyloid-β (Aβ) aggregates is found in the brains of Alzheimer's disease
patients. Thus, numerous efforts have been made to develop chemical reagents capable of …

[HTML][HTML] A turn for the worse: Aβ β-hairpins in Alzheimer's disease

SM Ruttenberg, JS Nowick - Bioorganic & Medicinal Chemistry, 2024 - Elsevier
Amyloid-β (Aβ) oligomers are a cause of neurodegeneration in Alzheimer's disease (AD).
These soluble aggregates of the Aβ peptide have proven difficult to study due to their …

Structural properties of Aβ (1–40) peptide in protonation stage of one, two, and three: New insights from the histidine protonation behaviors

Y Sun, Z Yao, H Shi - International Journal of Biological Macromolecules, 2022 - Elsevier
Structural properties and aggregation tendency can be significantly influenced by histidine
behaviors (histidine on N δ-H state is defined as δ, likewise, N ε-H: ε and both N δ-H and N ε …

Histidine protonation behaviors on structural properties and aggregation properties of Aβ (1–42) mature fibril: Approaching by edge effects

Y Sun, Y Shi, C Li, H Shi - The Journal of Physical Chemistry B, 2024 - ACS Publications
The histidine behavior plays a crucial role in the structural and aggregation properties of
protein folding and misfolding. Understanding the histidine behavior at the edge of the …

Insights into the effect of curcumin and (–)-epigallocatechin-3-gallate on the aggregation of Aβ (1–40) monomers by means of molecular dynamics

F Tavanti, A Pedone, MC Menziani - International Journal of Molecular …, 2020 - mdpi.com
In this study, we compared the effects of two well-known natural compounds on the early
step of the fibrillation process of amyloid-β (1–40), responsible for the formation of plaques …

Impact of A2V mutation and histidine tautomerism on Aβ42 monomer structures from atomistic simulations

H Li, Y Nam, A Salimi, JY Lee - Journal of Chemical Information …, 2020 - ACS Publications
The self-assembly of amyloid-β (Aβ) peptides into senile plaques in the brain is a hallmark of
Alzheimer's disease (AD) pathology. Mutation and histidine tautomerism are considered …

Small-Molecule Targeted Aβ42 Aggregate Degradation: Negatively Charged Small Molecules Are More Promising than the Neutral Ones

J Mei, H Yang, B Sun, C Liu, H Ai - ACS Chemical Neuroscience, 2021 - ACS Publications
Heavy evidence has confirmed that Aβ42 oligomers are the most neurotoxic aggregates and
play a critical role in the occurrence and development of Alzheimer's disease by causing …

Intrinsic origin of amyloid aggregation: collective effects of the mutation and tautomerism of histidine

H Li, A Salimi, JY Lee - ACS Chemical Neuroscience, 2019 - ACS Publications
Mutation is considered an important factor in the accumulation of amyloid-β (Aβ), which is a
hallmark of Alzheimer's disease (AD). A2V Aβ40 shows a higher aggregation tendency; …

Molecular mechanism of amyloidogenicity and neurotoxicity of a pro-aggregated tau mutant in the presence of histidine tautomerism via replica-exchange simulation

S Chatterjee, A Salimi, JY Lee - Physical Chemistry Chemical Physics, 2021 - pubs.rsc.org
The accumulation of ΔK280 tau mutant resulting in neurotoxic oligomeric aggregates is an
important but yet mysterious procedure in Alzheimer's disease (AD) development. Recently …

Structural and binding properties on Aβ mature fibrils due to the histidine tautomeric effect

H Shi, H Li, W Gong, R Gong, A Qian… - ACS Chemical …, 2019 - ACS Publications
Many studies have focused on histidine behaviors in misfolding diseases. However,
histidine behaviors on mature fibrils are still unknown. In the current study, we investigated …