Self-assembly of amyloidogenic peptides and their metal complexes are of multiple interest including their association with several neurological diseases. Therefore, a better understanding of the role of metal ions in the aggregation process is of broad interest. We report pH dependent structural and aggregation studies on ZnII binding to the amyloidogenic peptide Abeta 11-28. The results suggest that coordination of the N-terminal amine to ZnII is responsible for the inhibition of amyloid formation and the overall charge for amorphous aggregates.
Insights into the Mechanisms of Amyloid Formation of ZnII-Abeta 11-28: pH-Dependent Zinc Coordination and Overall Charge as Key Parameters for Kinetics and the Structure of ZnII-Abeta 11-28 Aggregates
LaPenna Giovanni;
2012
Abstract
Self-assembly of amyloidogenic peptides and their metal complexes are of multiple interest including their association with several neurological diseases. Therefore, a better understanding of the role of metal ions in the aggregation process is of broad interest. We report pH dependent structural and aggregation studies on ZnII binding to the amyloidogenic peptide Abeta 11-28. The results suggest that coordination of the N-terminal amine to ZnII is responsible for the inhibition of amyloid formation and the overall charge for amorphous aggregates.File in questo prodotto:
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