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  • Title: Transthyretin binding to A-Beta peptide--impact on A-Beta fibrillogenesis and toxicity.
    Author: Costa R, Gonçalves A, Saraiva MJ, Cardoso I.
    Journal: FEBS Lett; 2008 Mar 19; 582(6):936-42. PubMed ID: 18295603.
    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.
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