Structural perturbation of monomers determines the amyloid aggregation propersity of calcitonin and the variants

The initial structures of hCT (PDBid: 2jxz) and sCT (PDBid:2glh) used in our simulation are taken from the NMR structures solved in an aqueous solution. The phCT and TL-hCT are constructed using the PyMol mutagenesis based on the structure of hCT (PDBid: 2jxz). For each type of peptide, two molecular systems with one and five peptides were performed to investigate monomer conformation and self-assembly dynamics. For each molecular system, two independent all-atom DMD simulations were presented starting with different initial states (i.e., coordinates, orientations, and velocities). In five-peptide simulations, the initial configurations had a minimum intermolecular distance of more than 1.5 nm between any two molecules. The duration of each DMD trajectory in one- and five-peptide systems was 500 ns and 600 ns, respectively.  Initial conformations, input parameter and topology files for DMD simulation, and representative DMD output trajectories for each system are included in the upload data.