Abstract
In both senile systemic amyloidosis and familial amyloidotic polyneuropathy the amyloid fibrils are made up by full-length transthyretin (TTR) as well as fragments of the molecule. It has been demonstrated that other amyloid fibril proteins, e.g. atrial natriuretic factor and islet amyloid polypeptide can form amyloid-like fibrils in vitro. In the present study we have used both normal TTR, purified from plasma, and synthetic polypeptides, corresponding to segments of TTR. We show that normal TTR and two of the studied synthetic TTR segments easily form amyloid-like fibrils in vitro.
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