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 suuest 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.