Alzheimer’s disease (AD) is the most common presenile neurodegenerative disease. Causes of AD are not clearly elucidated yet. According to the amyloid hypothesis, amyloid beta deposits are the fundamental cause of the disease. Mutations in the Aß peptide alter the toxicity, oligomerization pathways and rate of fibril formation and can be grouped in pathogenic mutations and synthetic mutations. However, the precise mechanism of toxicity of amyloid aggregates remains unclear. Computational Molecular Modelling may help to clarify mechanisms behind aggregation and oligomerization of Aß. The present study focuses on conformational stability and mechanical properties of wild-type (WT) and mutants of amyloid β11-42.