  We employ a recently developed coarse-grained model for peptides and proteins
where the effect of pH is automatically included. We explore the effect of pH
in the aggregation process of the amyloidogenic peptide KTVIIE and two related
sequences, using three different pH environments. Simulations using large
systems (24 peptides chains per box) allow us to correctly account for the
formation of realistic peptide aggregates. We evaluate the thermodynamic and
kinetic implications of changes in sequence and pH upon peptide aggregation,
and we discuss how a minimalistic coarse-grained model can account for these
details.
