Amyloid oligomers: A joint experimental/computational perspective on Alzheimer's disease, Parkinson's disease, type II diabetes, and amyotrophic lateral sclerosis

PH Nguyen, A Ramamoorthy, BR Sahoo… - Chemical …, 2021 - ACS Publications
Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Structure and physicochemical properties of the Aβ42 tetramer: multiscale molecular dynamics simulations

HL Nguyen, P Krupa, NM Hai, HQ Linh… - The Journal of Physical …, 2019 - ACS Publications
Despite years of intensive research, little is known about oligomeric structures present
during Alzheimer's disease (AD). Excess of amyloid beta (Aβ) peptides and their …

Aggregation rate of amyloid beta peptide is controlled by beta-content in monomeric state

TTM Thu, NT Co, LA Tu, MS Li - The Journal of chemical physics, 2019 - pubs.aip.org
Understanding the key factors that govern the rate of protein aggregation is of immense
interest since protein aggregation is associated with a number of neurodegenerative …

The hazardous effects of the environmental toxic gases on amyloid beta-peptide aggregation: A theoretical perspective

V Saranya, PV Mary, S Vijayakumar, R Shankar - Biophysical Chemistry, 2020 - Elsevier
Alzheimer's disease (AD) is one of the leading causes of dementia in elderly people. It has
been well documented that the exposure to environmental toxins such as CO, CO 2, SO 2 …

[HTML][HTML] Effect of Bacterial Amyloid Protein Phenol− Soluble Modulin Alpha 3 on the Aggregation of Amyloid Beta Protein Associated with Alzheimer's Disease

B Peng, S Xu, Y Liang, X Dong, Y Sun - Biomimetics, 2023 - mdpi.com
Since the proposal of the brainstem axis theory, increasing research attention has been paid
to the interactions between bacterial amyloids produced by intestinal flora and the amyloid …

Emergence of barrel motif in amyloid-β trimer: a computational study

HL Nguyen, HQ Linh, P Matteini… - The Journal of …, 2020 - ACS Publications
Amyloid-β (Aβ) peptides form assemblies that are pathological hallmarks of Alzheimer's
disease. Aβ oligomers are soluble, mobile, and toxic forms of the peptide that act in the …

Computational design and evaluation of β‐sheet breaker peptides for destabilizing Alzheimer's amyloid‐β42 protofibrils

S Shuaib, SS Narang, D Goyal… - Journal of Cellular …, 2019 - Wiley Online Library
The β‐sheet breaker (BSB) peptides interfere with amyloid fibril assembly and used as
therapeutic agents in the treatment of Alzheimer's disease (AD). In this regard, a simple yet …

Kinetics and mechanical stability of the fibril state control fibril formation time of polypeptide chains: A computational study

M Kouza, NT Co, MS Li, S Kmiecik, A Kolinski… - The Journal of …, 2018 - pubs.aip.org
Fibril formation resulting from protein misfolding and aggregation is a hallmark of several
neurodegenerative diseases such as Alzheimer's and Parkinson's diseases. Despite much …

Zinc binding promotes greater hydrophobicity in Alzheimer's Aβ42 peptide than copper binding: Molecular dynamics and solvation thermodynamics studies

S Boopathi, P Dinh Quoc Huy… - Proteins: Structure …, 2020 - Wiley Online Library
The aggregation of Aβ42 peptides is considered as one of the main causes for the
development of Alzheimer's disease. In this context, Zn2+ and Cu2+ play a significant role in …

Impact of Mutations on the Conformational Transition from α-Helix to β-Sheet Structures in Arctic-Type Aβ40: Insights from Molecular Dynamics Simulations

RK Saini, S Shuaib, D Goyal, B Goyal - ACS omega, 2020 - ACS Publications
The amyloid-β (Aβ) protein aggregation into toxic oligomers and fibrils has been recognized
as a key player in the pathogenesis of Alzheimer's disease. Recent experiments reported …