Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-β Peptide Aggregation and Reduces the Toxicity of Its Oligomers
Seyyed Abolghasem Ghadami, Sean Chia, Francesco Simone Ruggeri, Georg Meisl, Francesco Bemporad, Johnny Habchi, Roberta Cascella, Christopher M. Dobson, Michele Vendruscolo, Tuomas P. J. Knowles, Fabrizio Chiti
Abstract
, while maintaining its overall topology. Hence, it is likely that the predominant mechanism by which TTR exerts its protective role lies in the binding of TTR to the Aβ oligomers and in inhibiting primary and secondary nucleation processes, which limits both the toxicity of Aβ oligomers and the ability of the fibrils to proliferate.
Topics & Concepts
TransthyretinFibrilThioflavinChemistryAmyloid (mycology)PeptideBiophysicsSenile plaquesAmyloid diseaseOligomerProtein foldingIn vitroBiochemistryAmyloid fibrilAlzheimer's diseaseBiologyAmyloid βDiseaseOrganic chemistryPathologyMedicineInorganic chemistryEndocrinologyAlzheimer's disease research and treatmentsAmyloidosis: Diagnosis, Treatment, OutcomesCellular transport and secretion