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  • Title: Unwinding fibril formation of medin, the peptide of the most common form of human amyloid.
    Author: Larsson A, Söderberg L, Westermark GT, Sletten K, Engström U, Tjernberg LO, Näslund J, Westermark P.
    Journal: Biochem Biophys Res Commun; 2007 Oct 05; 361(4):822-8. PubMed ID: 17679143.
    Abstract:
    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.
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