The aggregation of amyloid proteins into fibrils is associated with many neurodegenerative diseases such as Alzheimer's and Type II Diabetes. Extensive research has been spent in exploring different methods to impede and inhibit amyloid aggregation. Most attempts in the literature describe methods that involve applying stress to the environment around amyloids. Varying pH levels, modifying temperature, applying pressure through protein crowding and ligand docking are classical examples of these methods. However, environmental stress usually affects molecular pathways and protein functions in the cell and is challenging to construct in vivo. In this paper, we explore a new method to destabilize amyloid proteins through mutating their amino acid sequences without stressing their environment. We've developed FibrilMutant, a software aimed at exploring sequence mutations that destabilize amyloid fibrils. It analyzes key regions of amyloid proteins and studies the effect of amino acid point mutations on fibril nucleation and aggregation. The tool identified six main regions in amyloid proteins that contribute to structural stability and generated amino acid mutations to destabilize those regions. Full length fibrils were then built from the mutated amyloid monomers and a dipolar solvent model capturing the effect of dipole-dipole interactions between water and very large molecular systems to assess their aqueous stability was used to generate energy plots. Our results validate experimental mutation data for destabilizing Amylin fibrils and reveal novel point mutations that further weaken amylin amyloid nucleation and aggregation without disrupting the native structure.