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
2009 ◽  
Vol 113 (29) ◽  
pp. 9978-9987 ◽  
Author(s):  
V. Castelletto ◽  
I. W. Hamley ◽  
P. J. F. Harris ◽  
U. Olsson ◽  
N. Spencer

2010 ◽  
Vol 114 (2) ◽  
pp. 940-951 ◽  
Author(s):  
I. W. Hamley ◽  
D. R. Nutt ◽  
G. D. Brown ◽  
J. F. Miravet ◽  
B. Escuder ◽  
...  

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
V. Castelletto ◽  
P. Ryumin ◽  
R. Cramer ◽  
I. W. Hamley ◽  
M. Taylor ◽  
...  

RSC Advances ◽  
2014 ◽  
Vol 4 (32) ◽  
pp. 16517-16523 ◽  
Author(s):  
Keerthana Ramaswamy ◽  
Priyadharshini Kumaraswamy ◽  
Swaminathan Sethuraman ◽  
Uma Maheswari Krishnan

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.


RSC Advances ◽  
2018 ◽  
Vol 8 (73) ◽  
pp. 41705-41712 ◽  
Author(s):  
Son Tung Ngo ◽  
Huong Thi Thu Phung ◽  
Khanh B. Vu ◽  
Van V. Vu

Amyloid beta peptide oligomers are believed to play key roles in Alzheimer's disease pathogenesis. D23N mutation significantly changes their structure and how they bind potential inhibitors.


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