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Visualization of polymorphism in apolipoprotein C-II amyloid fibrils.
- Source :
-
Journal of Biochemistry . Jan2011, Vol. 149 Issue 1, p67-74. 8p. - Publication Year :
- 2011
-
Abstract
- The misfolding and self-assembly of proteins into amyloid fibrils, which occur in several debilitating and age-related diseases, are affected by common components of amyloid deposits, notably lipids and lipid complexes. Previously, the effects of phospholipids on amyloid fibril formation by apolipoprotein (apo) C-II have been examined, where low concentrations of micellar phospholipids and lipid bilayers induce a new, straight rod-like morphology for apoC-II fibrils. This fibril appearance is distinct from the twisted-ribbon morphology observed when apoC-II fibrils are formed in the absence of lipids. We used total internal reflection fluorescence microscopy (TIRFM) to visualize the described polymorphism of apoC-II amyloid fibrils. The spontaneous assembly of apoC-II into either twisted-ribbon fibrils in the absence of lipids or into fibrils of straight rod-like morphology when lipids are present was captured by TIRFM. The latter was found to be better suited for visualization using TIRFM. The difference between seeding of apoC-II straight fibrils on microscopic quartz slide and in test tube suggested a role for the effects of incubation surface on fibril formation. Seed-dependent growth of apoC-II straight fibrils was probed further by using a dual-labelling construct, giving insights into the straight fibril growth pattern. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 0021924X
- Volume :
- 149
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 79230851
- Full Text :
- https://doi.org/10.1093/jb/mvq117