Unwinding fibril formation of medin, the peptide of the most common form of human amyloid
- Department of Genetics and Pathology, Rudbeck Laboratory, Uppsala University, SE-75185 Uppsala (Sweden)
- Department of NVS, KASPAC, Karolinska Institute, Huddinge (Sweden)
- Division of Cell Biology, Diabetes Research Centre, Linkoeping University, Linkoeping (Sweden)
- Biotechnology Centre of Oslo, University of Oslo, Oslo (Norway)
- Ludwig Institute for Cancer Research, Uppsala (Sweden)
Medin amyloid affects the medial layer of the thoracic aorta of most people above 50 years of age. The consequences of this amyloid are not completely known but the deposits may contribute to diseases such as thoracic aortic aneurysm and dissection or to the general diminished elasticity of blood vessels seen in elderly people. We show that the 50-amino acid residue peptide medin forms amyloid-like fibrils in vitro. With the use of Congo red staining, Thioflavin T fluorescence, electron microscopy, and a solid-phase binding assay on different synthetic peptides, we identified the last 18-19 amino acid residues to constitute the amyloid-promoting region of medin. We also demonstrate that the two C-terminal phenylalanines, previously suggested to be of importance for amyloid formation, are not required for medin amyloid formation.
- OSTI ID:
- 21032906
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 361, Issue 4; Other Information: DOI: 10.1016/j.bbrc.2007.06.187; PII: S0006-291X(07)01416-7; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
Similar Records
Conversion of non-fibrillar {beta}-sheet oligomers into amyloid fibrils in Alzheimer's disease amyloid peptide aggregation
Polymer–Peptide Conjugates Disassemble Amyloid β Fibrils in a Molecular-Weight Dependent Manner