scholarly journals Amyloid peptides incorporating a core sequence from the amyloid beta peptide and gamma amino acids: relating bioactivity to self-assembly

2011 ◽  
Vol 47 (46) ◽  
pp. 12470 ◽  
Author(s):  
Valeria Castelletto ◽  
Ge Cheng ◽  
Ian W. Hamley
Keyword(s):  
Amino Acids ◽  
Amyloid Beta ◽  
Self Assembly ◽  
Amyloid Beta Peptide ◽  
Amyloid Peptides ◽  
Core Sequence ◽  
Beta Peptide

scholarly journals Curcumin Inhibits the Primary Nucleation of Amyloid-Beta Peptide: A Molecular Dynamics Study

Biomolecules ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1323
Author(s):  
Irini Doytchinova ◽  
Mariyana Atanasova ◽  
Evdokiya Salamanova ◽  
Stefan Ivanov ◽  
Ivan Dimitrov
Keyword(s):  
Molecular Dynamics ◽  
Hydrogen Bonds ◽  
Amyloid Beta ◽  
Amyloid Plaques ◽  
Amyloid Beta Peptide ◽  
Aβ Peptides ◽  
Amyloid Peptides ◽  
Primary Nucleation ◽  
Beta Peptide ◽  
Good Agreement

The amyloid plaques are a key hallmark of neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease. Amyloidogenesis is a complex long-lasting multiphase process starting with the formation of nuclei of amyloid peptides: a process assigned as a primary nucleation. Curcumin (CU) is a well-known inhibitor of the aggregation of amyloid-beta (Aβ) peptides. Even more, CU is able to disintegrate preformed Aβ firbils and amyloid plaques. Here, we simulate by molecular dynamics the primary nucleation process of 12 Aβ peptides and investigate the effects of CU on the process. We found that CU molecules intercalate among the Aβ chains and bind tightly to them by hydrogen bonds, hydrophobic, π–π, and cation–π interactions. In the presence of CU, the Aβ peptides form a primary nucleus of a bigger size. The peptide chains in the nucleus become less flexible and more disordered, and the number of non-native contacts and hydrogen bonds between them decreases. For comparison, the effects of the weaker Aβ inhibitor ferulic acid (FA) on the primary nucleation are also examined. Our study is in good agreement with the observation that taken regularly, CU is able to prevent or at least delay the onset of neurodegenerative disorders.

scholarly journals Self-Assembly and Anti-Amyloid Cytotoxicity Activity of Amyloid beta Peptide Derivatives

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
V. Castelletto ◽  
P. Ryumin ◽  
R. Cramer ◽  
I. W. Hamley ◽  
M. Taylor ◽  
...  
Keyword(s):  
Amyloid Beta ◽  
Self Assembly ◽  
Amyloid Beta Peptide ◽  
Cytotoxicity Activity ◽  
Beta Peptide ◽  
Peptide Derivatives

O2-03-01: Insight into the mechanism of gamma-secretase cleavage: Juxtamembrane amino acids are key to the length of secreted amyloid beta peptide

2010 ◽  
Vol 6 ◽  
pp. S100-S100
Author(s):  
Thomas Kukar ◽  
Thomas Ladd ◽  
Paul Robertson ◽  
Brenda Moore ◽  
Karen Jansen-West ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amyloid Beta ◽  
Amyloid Beta Peptide ◽  
Gamma Secretase ◽  
Beta Peptide ◽  
Insight Into

Influence of the Solvent on the Self-Assembly of a Modified Amyloid Beta Peptide Fragment. I. Morphological Investigation

2009 ◽  
Vol 113 (29) ◽  
pp. 9978-9987 ◽  
Author(s):  
V. Castelletto ◽  
I. W. Hamley ◽  
P. J. F. Harris ◽  
U. Olsson ◽  
N. Spencer
Keyword(s):  
Amyloid Beta ◽  
Self Assembly ◽  
The Self ◽  
Amyloid Beta Peptide ◽  
Peptide Fragment ◽  
Morphological Investigation ◽  
Beta Peptide

Self-assembly characteristics of a structural analogue of Tjernberg peptide

RSC Advances ◽  
2014 ◽  
Vol 4 (32) ◽  
pp. 16517-16523 ◽  
Author(s):  
Keerthana Ramaswamy ◽  
Priyadharshini Kumaraswamy ◽  
Swaminathan Sethuraman ◽  
Uma Maheswari Krishnan
Keyword(s):  
Amyloid Beta ◽  
Self Assembly ◽  
Amyloid Plaques ◽  
Amyloid Beta Peptide ◽  
Side Chains ◽  
Structural Analogue ◽  
Beta Peptide

This article aims to understand the pathogenesis behind the formation of amyloid plaques using a modified version of the KLVFF peptide. It was found that the cytotoxicity of the nanostructures formed by the RIVFF peptide may be attributed to the aminoacids with long side chains along with hydrophobic aminoacids resembling the amyloid beta peptide.

Self-assembly in aqueous solution of a modified amyloid beta peptide fragment

2008 ◽  
Vol 138 (1-2) ◽  
pp. 29-35 ◽  
Author(s):  
V. Castelletto ◽  
I.W. Hamley ◽  
P.J.F. Harris
Keyword(s):  
Aqueous Solution ◽  
Amyloid Beta ◽  
Self Assembly ◽  
Amyloid Beta Peptide ◽  
Peptide Fragment ◽  
Beta Peptide

scholarly journals Air/water Interface Induced Folding And Self-assembly Of Amyloid-beta Peptide

2009 ◽  
Vol 96 (3) ◽  
pp. 568a-569a
Author(s):  
Eva Y. Chi ◽  
Amy Winans ◽  
Shelli L. Frey ◽  
Kinlok Lam ◽  
Jaroslaw Majewski ◽  
...  
Keyword(s):  
Amyloid Beta ◽  
Self Assembly ◽  
Amyloid Beta Peptide ◽  
Water Interface ◽  
Induced Folding ◽  
Beta Peptide ◽  
Air Water Interface
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