Journal
CURRENT PHARMACEUTICAL DESIGN
Volume 14, Issue 30, Pages 3205-3218Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/138161208786404146
Keywords
Amyloid; beta 2-microglobulin; Dialysis-related amyloidosis; Amyloid beta; Protein misfolding; Total internal fluorescence microscopy
Categories
Funding
- CREST
- Japanese Ministry of Education, Culture, Sports, Science and Technology
- Japan Society for Promotion of Science (JSPS)
Ask authors/readers for more resources
Amyloid fibrils have been a critical subject in recent studies of proteins since they are associated with the pathology of more than 20 serious human diseases. Moreover, a variety of proteins and peptides not related to diseases are able to form amyloid fibrils or amyloid-like structures, implying that amyloid formation is a generic property of polypeptides. Although understanding the structure and formation of amyloid fibrils is crucial, due to the extremely high molecular weight and insolubility of amyloid fibrils, most of the conventional techniques available for soluble proteins are not directly applicable to these fibrils. However, structural studies using solid-state NMR have shown that the basic motif of amyloid fibrils is a beta-strand-loop-beta-strand conformation often in a parallel beta-sheet assembly. From the hydrogen/deuterium exchange of amide protons, amyloid fibrils have been shown to be stabilized by an extensive network of hydrogen bonds substantiating sheets. Our approach using total internal reflection fluorescence microscopy combined with thioflavin T, an amyloid-specific fluorescence dye, enabled monitoring fibril growth in real-time at single fibril level. On the basis of these various approaches, increasingly convincing models of amyloid structures, their formation and propagation are emerging.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available