These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Dissection of the key steps of amyloid-β peptide 1-40 fibrillogenesis.
    Author: Leite JP, Gimeno A, Taboada P, Jiménez-Barbero JJ, Gales L.
    Journal: Int J Biol Macromol; 2020 Dec 01; 164():2240-2246. PubMed ID: 32771514.
    Abstract:
    The aggregation kinetics of Aβ1-40 peptide was characterized using a synergistic approach by a combination of nuclear magnetic resonance, thioflavin-T fluorescence, transmission electron microscopy and dynamic light scattering. A major finding is the experimental detection of high molecular weight oligomers (HMWO) that converts into fibrils nuclei. Our observations are consistent with a mechanism of Aβ1-40 fibrillogenesis that includes the following key steps: i) slow formation of HMWO (Rh ~ 20 nm); ii) conversion of the HMWO into more compact Rh ~ 10 nm fibrils nuclei; iii) fast formation of additional fibrils nuclei through fibril surface catalysed processes; and iv) growth of fibrils by addition of soluble Aβ species. Moreover, NMR diffusion experiments show that at 37 °C soluble Aβ1-40 remains intrinsically disordered and mostly in monomeric form despite evidences of the presence of dimers and/or other small oligomers. A mathematical model is proposed to simulate the aggregation kinetics of Aβ1-40.
    [Abstract] [Full Text] [Related] [New Search]