| Literature DB >> 18295603 |
R Costa1, A Gonçalves, M J Saraiva, I Cardoso.
Abstract
It has been suggested that transthyretin (TTR) is involved in preventing A-Beta fibrillization in Alzheimer's disease (AD). Here, we characterized the TTR/A-Beta interaction by competition binding assays. TTR binds to different A-Beta peptide species: soluble (Kd, 28 nM), oligomers and fibrils; diverse TTR variants bind differentially to A-Beta. Transmission electron microscopy (TEM) analysis demonstrated that TTR is capable of interfering with A-Beta fibrillization by both inhibiting and disrupting fibril formation. Co-incubation of the two molecules resulted in the abolishment of A-Beta toxicity. Our results confirmed TTR as an A-Beta ligand and indicated the inhibition/disruption of A-Beta fibrils as a possible mechanism underlying the protective role of TTR in AD.Entities:
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Year: 2008 PMID: 18295603 DOI: 10.1016/j.febslet.2008.02.034
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124