Аннотация:Alzheimer's diseaseis the most common neurodegenerative disorder having escalating global importance. Epidemiological forecast predicts substantial growth of both number of affected individualsand the pathology impact onto mortality allovertheglobe.Despiteunprecedented efforts of researchers and medical professionals, the only treatment available is fairly symptomatic and hardly effective [1]. The hampered results are likely due tosimultaneous involvement oftwo molecular pathogenesis factors:amyloid beta and tau-protein. The Alzheimer's neurodegenerationpathway involves a sophisticated interplay of these. The interactions are inthat one toxic agent iscapable of transferring its pathologic state to the other with amyloid beta byprion-like mechanism. Amyloid beta appears to have an initiator role as it triggers the downstream pathogenesis part [2].The advances of the research rely largely on modelling techniques enabling insights intostructural and mechanistic bases for amyloid formation of both amyloidbeta and other neurodegeneration-related peptides. Studyingmodel protein systems thatare not directly connected to the pathology can shed an additional light as well.Here weattempted to establish impacts of distinct structural andphysical characteristics by considering experimental as well as computational data on them in relation to aparticular amino acid sequence. This enabled us to assess their correlation in amyloidogenic peptides and to rank them by impact.