Influence of the Solvent on the Self-Assembly of a Modified Amyloid Beta Peptide Fragment. II. NMR and Computer Simulation Investigation

2010 ◽  
Vol 114 (2) ◽  
pp. 940-951 ◽  
Author(s):  
I. W. Hamley ◽  
D. R. Nutt ◽  
G. D. Brown ◽  
J. F. Miravet ◽  
B. Escuder ◽  
...  
Keyword(s):  
Computer Simulation ◽  
Amyloid Beta ◽  
Self Assembly ◽  
The Self ◽  
Amyloid Beta Peptide ◽  
Peptide Fragment ◽  
Beta Peptide

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 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

Molecular dynamics studies of a β-sheet blocking peptide with the full-length amyloid beta peptide of Alzheimer’s disease

2016 ◽  
Vol 94 (10) ◽  
pp. 833-841 ◽  
Author(s):  
Zohreh Amini ◽  
Mohammad Hossein Fatemi ◽  
Arvi Rauk
Keyword(s):  
Alzheimer’S Disease ◽  
Molecular Dynamics ◽  
Amyloid Beta ◽  
Recognition Site ◽  
Full Length ◽  
The Self ◽  
Amyloid Beta Peptide ◽  
Self Recognition ◽  
Beta Peptide ◽  
Β Sheet

The region encompassing residues 13–23 of the amyloid beta peptide (Aβ(13–23)) of Alzheimer’s disease is the self-recognition site that initiates toxic oligomerization and fibrillization. A number of pseudopeptides have been designed to bind to Aβ(13–23) and been computationally shown to do so with high affinity. More interactions are available in full-length Aβ than are available in the shorter peptide. We describe herein a study by molecular dynamics (MD) of nine distinct complexes formed by one such pseudopeptide, SGA1, with full-length beta amyloid, Aβ(1–42). The relative stabilities of the Aβ–SGA1 complexes were estimated by a combination of MD and ab initio methods. The most stable complex, designated AB1, was found to be one in which SGA1 is bound to the self-recognition site of Aβ(1–42) in an antiparallel β-sheet fashion. Another complex, designated AB3, also involved SGA1 binding to the self-recognition region of Aβ(1–42), albeit with lower affinity. In both AB1 and AB3, SGA1 formed antiparallel β-sheets but to opposite edges of Aβ. A complex, AB4, with similar stability to AB3, was found with a parallel β-sheet in the self-recognition site. A fourth complex, AB7, also with similar stability, formed a parallel β-sheet in the hydrophobic central region of Aβ. In all cases, complexation of SGA1 induced extensive β-sheet structure in Aβ(1–42).

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

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.

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