Amyloidosis is a subtle systemic group of disease symbolized by disordered form of abnormal precursor proteins inducing accumulation of ambiguous auto aggregates causing amyloid fibril formation in a prevalent β-pleated sheet structure. Alzheimer’s disease (AD) and Type 2 diabetes (T2D) are the two utmost prevailing and debilitating neurodegenerative disorders among aging individuals Both AD and T2D are described by insoluble protein amyloid aggregates having fibrillar structures formed by amyloid-β (Aβ) and human islet amyloid polypeptide (hIAPP), respectively. In order to understand the conformational dynamics of these amyloidogenic proteins or peptides and the strategy of conformational ensemble recognition for various binding residues and small inhibitors, an advanced sampling in silico technique, "replica exchange molecular dynamics (REMD)" has been used accompanied by experimental validations. An important factor that affects protein folding and interactions with cell membranes and interfaces, is the presence of small co-solutes or osmolytes that influence and counterbalance the osmotic pressure of the cell and its environment. Drug repurposing is a rapid and secure strategy for determining new usage of approved drugs for treating another disease and this can be beneficial in discovering new anti-aggregating compounds from pre-existing approved drugs. Our study implements atomistic observations of conformational ensemble under the influence of osmolytes as denaturants and counter denaturants which modulates Aβ and hIAPP peptides. We have discovered repurposed drugs for AD associated Aβ amyloidosis and T2D associated hIAPP amyloidosis. A common compound showing dual inhibition against Aβ and hIAPP amyloidosis that would treat both AD and T2D has also been identified through our study. In immense view, the repurposed drugs as potent inhibitors may serve as the leading structural template for future development of more anti-amyloidogenic compounds.