Structural analysis of peptide fragment 71-93 of transthyretin by NMR spectroscopy and electron microscopy: Insight into amyloid fibril formation

Biochemistry ◽  
1994 ◽  
Vol 33 (1) ◽  
pp. 33-41 ◽  
Author(s):  
Jacqueline A. Jarvis ◽  
Sharon L. A. Munro ◽  
David J. Craik
Keyword(s):  
Electron Microscopy ◽  
Nmr Spectroscopy ◽  
Structural Analysis ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Peptide Fragment ◽  
Amyloid Fibril Formation ◽  
Insight Into

scholarly journals Novel Transthyretin Amyloid Fibril Formation Inhibitors: Synthesis, Biological Evaluation, and X-Ray Structural Analysis

PLoS ONE ◽  
2009 ◽  
Vol 4 (7) ◽  
pp. e6290 ◽  
Author(s):  
Satheesh K. Palaninathan ◽  
Nilofar N. Mohamedmohaideen ◽  
Elisabetta Orlandini ◽  
Gabriella Ortore ◽  
Susanna Nencetti ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Amyloid Fibril ◽  
Biological Evaluation ◽  
Fibril Formation ◽  
X Ray ◽  
Amyloid Fibril Formation

scholarly journals 2P114 Amyloid fibril formation of a peptide fragment of transthyretin(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

2006 ◽  
Vol 46 (supplement2) ◽  
pp. S324
Author(s):  
Makoto Takeuchi ◽  
Mineyuki Mizuguchi ◽  
Mizuki Dobashi ◽  
Yoshihiro Mori ◽  
Hiroyuki Shinoda ◽  
...  
Keyword(s):  
Protein Folding ◽  
Poster Session ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Peptide Fragment ◽  
Meeting Program ◽  
Amyloid Fibril Formation

The Influence of Ca2+ and Zn2+ on the Amyloid Fibril Formation by β-Casein

2020 ◽  
Vol 27 (9) ◽  
pp. 915-922
Author(s):  
Jia Wang ◽  
Jihua Liu ◽  
Guangguang Du ◽  
Yang An ◽  
Chunfang Zhao ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Intrinsic Fluorescence ◽  
Amyloid Fibril Formation ◽  
Transmission Electron ◽  
Concentration Changes ◽  
Set Up ◽  
The Relationship ◽  
Different Tissues

Background: The amyloid fibril formation in different tissues or organs is related to amyloidosis. The Ca2+, Zn2+ and heparan sulfate (HS) are important elements and compositions in human body, which play a key role in regulating various physiological activities. Recently, there are increasing evidence suggest that they are closely linked to the amyloid fibril formation. Objective: The effect of Ca2+ and Zn2+ on the amyloid fibril formation by β-casein was investigated in the absence and presence of HS, which was significantly to explore the relationship between the concentration changes of Ca2+ and Zn2+ and amyloid fibril formation. Method: In this work, the influence of Ca2+ and Zn2+ on the β-casein fibril formation in the absence and presence of HS was investigated by various methods of Thioflavin T fluorescence assay, transmission electron microscopy and intrinsic fluorescence measure. Results: The results demonstrated that Ca2+ and Zn2+ promoted the β-casein fibril formation. The effect of Ca2+ was greater than that of Zn2+. Meanwhile, the both metal ions had stronger effects when β-casein was incubated with HS together. In addition, it was also observed that the microenvironment of β-casein was changed because the intrinsic fluorescence peaks were red-shifted on the influence of Ca2+ and Zn2+. Conclusion: Ca2+ and Zn2+ were capable of promoting the β-casein fibril formation in the both absence and presence of HS. This work set up the foundation for further researching of the amyloidosis pathogenesis and provided new insight for us to understand relationship between the inflammation and amyloidosis.

scholarly journals Amyloid as a natural product

2003 ◽  
Vol 161 (3) ◽  
pp. 461-462 ◽  
Author(s):  
Jeffery W. Kelly ◽  
William E. Balch
Keyword(s):  
Natural Product ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Integral Membrane Protein ◽  
Fibril Formation ◽  
Proteolytic Processing ◽  
Biological Pathway ◽  
Peptide Fragment ◽  
Amyloid Fibril Formation ◽  
Amyloid Diseases

Amyloid fibrils, such as those found in Alzheimer's and the gelsolin amyloid diseases, result from the misassembly of peptides produced by either normal or aberrant intracellular proteolytic processing. A paper in this issue by Marks and colleagues (Berson et al., 2003) demonstrates that intra-melanosome fibrils are formed through normal biological proteolytic processing of an integral membrane protein. The resulting peptide fragment assembles into fibrils promoting the formation of melanin pigment granules. These results, along with the observation that amyloid fibril formation by bacteria is highly orchestrated, suggest that fibril formation is an evolutionary conserved biological pathway used to generate natural product nanostructures.

Immunocytochemical Localization of Amyloid Protein AA in the “Dense Fibrillar Inclusions” of the Reticuloendothelical Cells

1977 ◽  
Vol 35 ◽  
pp. 438-439
Author(s):  
T. Shirahama ◽  
M. Skinner ◽  
A.S. Cohen
Keyword(s):  
Amyloid Fibril ◽  
Close Association ◽  
Gel Filtration ◽  
Fibril Formation ◽  
Amyloid Protein ◽  
Electron Microscopic ◽  
Amyloid Deposits ◽  
Amyloid Fibril Formation ◽  
Electron Microscopic Technique ◽  
Lysosomal System

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.

Effect of pH and inhibitors on beta-amyloid fibril assembly

1996 ◽  
Vol 54 ◽  
pp. 752-753
Author(s):  
Beverly E. Maleeff ◽  
Timothy K. Hart ◽  
Stephen J. Wood ◽  
Ronald Wetzel
Keyword(s):  
Amyloid Fibril ◽  
Peptide Fragment ◽  
Hydrophobic Peptides ◽  
Amyloid Fibril Formation ◽  
Effects Of Ph ◽  
Severity Of The Disease ◽  
Kinetics Of ◽  
The Brain

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.

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