β-Sheeted Amyloid Fibril Based Structures For Hybrid Nanoobjects On Solid Surfaces

Author(s):  
V. Bukauskas ◽  
V. Strazdienė ◽  
A. Šetkus ◽  
S. Bružytė ◽  
V. Časaitė ◽  
...  
Author(s):  
T. Shirahama ◽  
M. Skinner ◽  
A.S. Cohen

A1thought the mechanisms of amyloidogenesis have not been entirely clarified, proteolysis of the parent proteins may be one of the important steps in the amyloid fibril formation. Recently, we reported that "dense fibrillar inclusions" (DFI), which had the characteristics of lysosomes and contained organized fibrillar profiles as well, were observed in the reticuloendothelial cells in close association with the foci of new amyloid deposits. We considered the findings as evidence for the involvement of lysosomal system in amyloid fibril formation (l). In the present study, we attempted to determine the identity of the contents of the DFI by the use of antisera against the amyloid protein (AA) and an immuno-electron microscopic technique.Amyloidosis was induced in CBA/J mice by daily injections of casein (l). AA was isolated from amyloid-laden spleens by gel filtration and antibody to it was produced in rabbits (2). For immunocytochemistry, the unlabeled antibody enzyme method (3) was employed.


Author(s):  
Beverly E. Maleeff ◽  
Timothy K. Hart ◽  
Stephen J. Wood ◽  
Ronald Wetzel

Alzheimer's disease is characterized post-mortem in part by abnormal extracellular neuritic plaques found in brain tissue. There appears to be a correlation between the severity of Alzheimer's dementia in vivo and the number of plaques found in particular areas of the brain. These plaques are known to be the deposition sites of fibrils of the protein β-amyloid. It is thought that if the assembly of these plaques could be inhibited, the severity of the disease would be decreased. The peptide fragment Aβ, a precursor of the p-amyloid protein, has a 40 amino acid sequence, and has been shown to be toxic to neuronal cells in culture after an aging process of several days. This toxicity corresponds to the kinetics of in vitro amyloid fibril formation. In this study, we report the biochemical and ultrastructural effects of pH and the inhibitory agent hexadecyl-N-methylpiperidinium (HMP) bromide, one of a class of ionic micellar detergents known to be capable of solubilizing hydrophobic peptides, on the in vitro assembly of the peptide fragment Aβ.


1985 ◽  
Vol 10 (6) ◽  
pp. 893-900 ◽  
Author(s):  
S.B. Crampton

1994 ◽  
Vol 4 (1) ◽  
pp. 59-73 ◽  
Author(s):  
Z. M. Sun ◽  
J. M. Engels ◽  
I. Dozov ◽  
G. Durand

1983 ◽  
Vol 139 (4) ◽  
pp. 736
Author(s):  
V.N. Ageev ◽  
E.Ya. Zandberg ◽  
N.I. Ionov ◽  
A.Ya. Tontegode

2003 ◽  
Vol 771 ◽  
Author(s):  
G. Panzera ◽  
S. Conoci ◽  
S. Coffa ◽  
B. Pignataro ◽  
S. Sortino ◽  
...  

AbstractThin films (1-24 layers) of bis-zinc ethane-bridged porphyrin dimer (1) have been transferred on solid surfaces, by the Langmuir- Schäfer (LS) horizontal method. The related surface pressurearea isotherm curve shows that in dependence of the film pressure different condensed phases may occur in the monolayer. The inspection of the monolayer by Brewster Angle Microscopy (BAM) reveals the presence of peculiar networks whose structural features seemingly change upon film compression. On the other hand, the Scanning Force Microscopy (SFM) analysis performed on LS films shows fractal networks constituted by nanoscopic supramolecular aggregates, whose shape and size depend again on the LS deposition surface pressure. Finally, also UV-vis spectroscopy measurements indicates that the absorption is almost linearly related to the film thickness that is directly connected to the surface pressure.


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