Role of the region 23-28 in Aβ fibril formation: insights from simulations of the monomers and dimers of Alzheimer's peptides Aβ40 and Aβ42
A Melquiond, X Dong, N Mousseau… - Current Alzheimer …, 2008 - ingentaconnect.com
Self-assembly of the 40/42 amino acid Aβ peptide is a key player in Alzheimer's disease.
Aβ40 is the most prevalent species, while Aβ42 is the most toxic. It has been suggested that …
Aβ40 is the most prevalent species, while Aβ42 is the most toxic. It has been suggested that …
Computational simulations of the early steps of protein aggregation
G Wei, N Mousseau, P Derreumaux - Prion, 2007 - Taylor & Francis
There is strong evidence that the oligomers of key proteins, formed during the early steps of
aggregation, could be the primary toxic species associated with human neurodegenerative …
aggregation, could be the primary toxic species associated with human neurodegenerative …
Effect of surfaces on amyloid fibril formation
Using atomic force microscopy (AFM) we investigated the interaction of amyloid beta (Aβ)(1–
42) peptide with chemically modified surfaces in order to better understand the mechanism …
42) peptide with chemically modified surfaces in order to better understand the mechanism …
Thermodynamics and dynamics of amyloid peptide oligomerization are sequence dependent
Y Lu, P Derreumaux, Z Guo… - Proteins: Structure …, 2009 - Wiley Online Library
Aggregation of the full‐length amyloid‐β (Aβ) and β2‐microglobulin (β2m) proteins is
associated with Alzheimer's disease and dialysis‐related amyloidosis, respectively. This …
associated with Alzheimer's disease and dialysis‐related amyloidosis, respectively. This …
NFGAIL amyloid oligomers: the onset of beta-sheet formation and the mechanism for fibril formation
W Hoffmann, K Folmert, J Moschner… - Journal of the …, 2018 - ACS Publications
The hexapeptide NFGAIL is a highly amyloidogenic peptide, derived from the human islet
amyloid polypeptide (hIAPP). Recent investigations indicate that presumably soluble hIAPP …
amyloid polypeptide (hIAPP). Recent investigations indicate that presumably soluble hIAPP …
Exploring the Influence of Carbon Nanoparticles on the Formation of β-Sheet-Rich Oligomers of IAPP22–28 Peptide by Molecular Dynamics Simulation
Recent advances in nanotechnologies have led to wide use of nanomaterials in biomedical
field. However, nanoparticles are found to interfere with protein misfolding and aggregation …
field. However, nanoparticles are found to interfere with protein misfolding and aggregation …
hIAPP-Amyloid-Core Derived d-Peptide Prevents hIAPP Aggregation and Destabilizes Its Protofibrils
The aberrant misfolding of human islet amyloid polypeptide into cytotoxic amyloid
aggregates is the hallmark of type II diabetes. In order to avert the formation of amyloid …
aggregates is the hallmark of type II diabetes. In order to avert the formation of amyloid …
Self-assembly of the β2-microglobulin NHVTLSQ peptide using a coarse-grained protein model reveals a β-barrel species
Although a wide variety of proteins can assemble into amyloid fibrils, the structure of the
early oligomeric species on the aggregation pathways remains unknown at an atomic level …
early oligomeric species on the aggregation pathways remains unknown at an atomic level …
Potential of ATP toward Prevention of hIAPP oligomerization and destabilization of hIAPP protofibrils: An in silico perspective
The aggregation of an intrinsically disordered protein, human islet amyloid polypeptide
(hIAPP), leads to one of the most prevalent endocrine disorders, type II diabetes mellitus …
(hIAPP), leads to one of the most prevalent endocrine disorders, type II diabetes mellitus …
Disparate effect of hybrid peptidomimetics containing isomers of aminobenzoic Acid on hIAPP aggregation
The abnormal misfolding of human islet amyloid polypeptide (hIAPP) in pancreatic β-cells is
implicated in the progression of type II diabetes (T2D). With the prevalence of T2D …
implicated in the progression of type II diabetes (T2D). With the prevalence of T2D …