Insights into the Mechanisms of Amyloid Formation of ZnII-Ab11-28: pH-Dependent Zinc Coordination and Overall Charge as Key Parameters for Kinetics and the Structure of ZnII-Ab11-28 Aggregates

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 Zn(II) binding to the amyloidogenic peptide Ab11-28. The results suggest that coordination of the N-terminal amine to Zn(II) is responsible for the inhibition of amyloid formation and the overall charge for amorphous aggregates.