Article
Effects of the known pathogenic mutations on the aggregation pathway of the amyloidogenic peptide of apolipoprotein A-I.
Journal of molecular biology - 1 Apr 2011
Raimondi Sara, Guglielmi Fulvio, Giorgetti Sofia, Di Gaetano Sonia, Arciello Angela, Monti Daria M, Relini Annalisa, Nichino Daniela, Doglia Silvia M, Natalello Antonino, Pucci Piero, Mangione Palma, Obici Laura, Merlini Giampaolo, Stoppini Monica, Robustelli Paul, Tartaglia Gian Gaetano, Vendruscolo Michele, Dobson Christopher M, Piccoli Renata, Bellotti Vittorio
Abstract excerpt
The 93-residue N-terminal fragment of apolipoprotein A-I (ApoA-I) is the major constituent of fibrils isolated from patients affected by the amyloidosis caused by ApoA-I mutations. We have prepared eight polypeptides corresponding to all the currently known amyloidogenic variants of the N-terminal region of ApoA-I, other than a truncation mutation, and investigated their aggregation kinetics and the associated...
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