In this scenario, the formation of amyloid fibrils is driven by αSyn conformations with an optimally minimized set of unfavourable electrostatic interactions and maximization of favourable interactions to ensure fibril stability under such unfavourable conditions. In other words, structural polymorphism is primarily influenced by thermodynamic stability of the resulting fibrils. These polymorphs exhibit enhanced stability compared to the kinetically controlled ones when transferred to the conditions where electrostatic forces are attenuated (high salt). The NS polymorph represents a low and possibly the global energy minimum on the rugged conformational landscape for neutral pH conditions which is unlikely to be sampled in the physiologically relevant context due to the easier accessibility of other fibril morphologies at physiological ionic strength. However, it provides important insights into the delicate interplay between kinetic and thermodynamic factors and their influence on fibril stability and polymorphism.