Structure Comparison of Beta Amyloid Peptide Aβ 1–42 Isoforms. Molecular Dynamics Modeling

AP Tolstova, AA Makarov… - Journal of Chemical …, 2024 - ACS Publications
Beta amyloid peptide Aβ 1–42 (Aβ42) has a unique dual role in the human organism, as
both the peptide with an important physiological function and one of the most toxic biological …

Conformational changes of Aβ (1–42) monomers in different solvents

M Lee, HJ Chang, JY Park, J Shin, JW Park… - Journal of Molecular …, 2016 - Elsevier
Amyloid proteins are known to be the main cause of numerous degenerative and
neurodegenerative diseases. In general, amyloids are misfolded from monomers and they …

In silico investigation on the inhibition of Aβ42 aggregation by Aβ40 peptide by potential of mean force study

M Dutta, VSK Mattaparthi - Journal of Biomolecular Structure and …, 2018 - Taylor & Francis
Recent experimental data revealed that small, soluble Amyloid beta (Aβ42) oligomers,
especially dimers impair synaptic plasticity and memory leading to Alzheimer's disease …

Structures of the Amyloid β-Peptides Aβ1–40 and Aβ1–42 as Influenced by pH and a d-Peptide

OO Olubiyi, B Strodel - The Journal of Physical Chemistry B, 2012 - ACS Publications
In this simulation study, we present a comparison of the secondary structure of the two major
alloforms of the Alzheimer's peptide (Aβ1–40 and Aβ1–42) on the basis of molecular …

Modulation in the conformational and stability attributes of the Alzheimer's disease associated amyloid-beta mutants and their favorable stabilization by curcumin …

M Awasthi, S Singh, VP Pandey… - Journal of Biomolecular …, 2018 - Taylor & Francis
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by progressive
accumulation of amyloid-beta (Aβ) peptides in brain. In the present study, two familial Aβ42 …

Comparing the folding free‐energy landscapes of Aβ42 variants with different aggregation properties

S Mitternacht, I Staneva, T Härd… - … : Structure, Function, and …, 2010 - Wiley Online Library
The properties of the amyloid‐β peptide that lead to aggregation associated with Alzheimer's
disease are not fully understood. This study aims at identifying conformational differences …

Folding events in the 21-30 region of amyloid β-protein (Aβ) studied in silico

JM Borreguero, B Urbanc, ND Lazo… - Proceedings of the …, 2005 - National Acad Sciences
Oligomeric assemblies of the amyloid β-protein (Aβ) have been implicated in the
pathogenesis of Alzheimer's disease as a primary source of neurotoxicity. Recent in vitro …

Molecular Simulation of the amyloid β-peptide Aβ-(1-40) of Alzheimer's disease

PP Mager - Molecular Simulation, 1998 - Taylor & Francis
Abstract The amyloid Aβ (1–40) peptide of Alzheimer's disease was chosen as model
compound. This Aβ peptide is an intrinsically soluble peptide; the C-terminal amino acids …

Effects of the Arctic (E22→G) Mutation on Amyloid β-Protein Folding: Discrete Molecular Dynamics Study

AR Lam, DB Teplow, HE Stanley… - Journal of the American …, 2008 - ACS Publications
The 40–42 residue amyloid β-protein (Aβ) plays a central role in the pathogenesis of
Alzheimer's disease (AD). Of the two main alloforms, Aβ40 and Aβ42, the longer Aβ42 is …

Targeted studies on the interaction of nicotine and morin molecules with amyloid β-protein

S Boopathi, P Kolandaivel - Journal of molecular modeling, 2014 - Springer
Alzheimer's disease (AD) is a neurodegenerative disorder that occurs due to progressive
deposition of amyloid β-protein (Aβ) in the brain. Stable conformations of solvated Aβ 1-42 …