Figure 5.

Proposed mechanism of the formation of polymorphs based on the diversity of steric zippers. (a) Tau amyloid polymorphs from Alzheimer’s and Pick’s disease patients, showing difference in protofilament folds. Schematic illustrations of the arrangements of side chains in this panel are redrawn based on those in [23,24]. Hydrophobic, polar, positively charged, and negatively charged residues are colored by white, green, blue, and red, respectively. (b) Tau amyloid polymorphs from Alzheimer’s patients, PHF and SF, showing differences in the arrangement of interactions of two protofilaments. Red arrows indicate electron densities attributed to the interaction with the side chains of K³¹⁷ and K³²¹. Reproduced with modification from [23], with permission. Copyright (2017) Springer Nature.