Peptides composed of alternating L-and D-amino acids inhibit amyloidogenesis in three distinct amyloid systems independent of sequence
There is now substantial evidence that soluble oligomers are primary toxic agents in amyloid
diseases. The development of an antibody recognizing the toxic soluble oligomeric forms of …
diseases. The development of an antibody recognizing the toxic soluble oligomeric forms of …
Designed α-sheet peptides inhibit amyloid formation by targeting toxic oligomers
Previous studies suggest that the toxic soluble-oligomeric form of different amyloid proteins
share a common backbone conformation, but the amorphous nature of this oligomer …
share a common backbone conformation, but the amorphous nature of this oligomer …
[HTML][HTML] Focus: medical technology: the role of α-sheet in amyloid oligomer aggregation and toxicity
A major barrier to developing effective treatments and diagnostics for amyloid diseases is
the inability of traditional protein structure characterization methods to elucidate the structure …
the inability of traditional protein structure characterization methods to elucidate the structure …
A molecular dynamics study of the interaction of D-peptide amyloid inhibitors with their target sequence reveals a potential inhibitory pharmacophore conformation
The self-assembly of soluble proteins and peptides into β-sheet-rich oligomeric structures
and insoluble fibrils is a hallmark of a large number of human diseases known as amyloid …
and insoluble fibrils is a hallmark of a large number of human diseases known as amyloid …
Chemical and Physical Variability in Structural Isomers of an l/d α-Sheet Peptide Designed To Inhibit Amyloidogenesis
There has been much interest in synthetic peptides as inhibitors of aggregation associated
with amyloid diseases. Of particular interest are compounds that target the cytotoxic soluble …
with amyloid diseases. Of particular interest are compounds that target the cytotoxic soluble …
Molecular dynamics simulations of alanine rich β‐sheet oligomers: Insight into amyloid formation
B Ma, R Nussinov - Protein Science, 2002 - Wiley Online Library
The aggregation observed in protein conformational diseases is the outcome of significant
new β‐sheet structure not present in the native state. Peptide model systems have been …
new β‐sheet structure not present in the native state. Peptide model systems have been …
Elongation of ordered peptide aggregate of an amyloidogenic hexapeptide NFGAIL observed in molecular dynamics simulations with explicit solvent
The mechanisms by which amyloidogenic peptides and proteins form soluble toxic
oligomers remain elusive. We have studied the formation of partially ordered tetramers and …
oligomers remain elusive. We have studied the formation of partially ordered tetramers and …
A hairpin motif in the amyloid-β peptide is important for formation of disease-related oligomers
The amyloid-β (Aβ) peptide is associated with the development of Alzheimer's disease and
is known to form highly neurotoxic prefibrillar oligomeric aggregates, which are difficult to …
is known to form highly neurotoxic prefibrillar oligomeric aggregates, which are difficult to …
α-Sheet: the toxic conformer in amyloid diseases?
V Daggett - Accounts of chemical research, 2006 - ACS Publications
A novel secondary structure, the α-sheet, was identified through molecular dynamics (MD)
simulations of various proteins associated with amyloid diseases under amyloidogenic …
simulations of various proteins associated with amyloid diseases under amyloidogenic …
Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis
A Lakshmanan, DW Cheong… - Proceedings of the …, 2013 - National Acad Sciences
The self-assembly of abnormally folded proteins into amyloid fibrils is a hallmark of many
debilitating diseases, from Alzheimer's and Parkinson diseases to prion-related disorders …
debilitating diseases, from Alzheimer's and Parkinson diseases to prion-related disorders …