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Unwinding fibril formation of medin, the peptide of the most common form of human amyloid
Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Division of cell biology.
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2007 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 361, no 4, 822-828 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2007. Vol. 361, no 4, 822-828 p.
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Medical and Health Sciences
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URN: urn:nbn:se:liu:diva-40479DOI: 10.1016/j.bbrc.2007.06.187Local ID: 53358OAI: oai:DiVA.org:liu-40479DiVA: diva2:261328
Available from: 2009-10-10 Created: 2009-10-10 Last updated: 2017-12-13

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Westermark, Gunilla

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