The growth of amyloid β peptides arises from inappropriate cleavage of amyloid precursor protein that induces the formation of amyloid plaques in the brain. An excessive accumulation of amyloid β plaques promotes the development of dementia, specifically Alzheimer’s disease (AD). Histopathological evidence suggested that insulin resistance and type 2 diabetes condition have a stronger correlation with Alzheimer’s disease development. An increasing concentration of amyloid β leads to impaired binding of insulin to its receptor. Previous studies suggested that the monomeric form of amyloid β was the potential molecule, which can compete with insulin for receptor binding. The objective of this work was to study the molecular interactions of insulin and amyloid β to insulin receptors using protein-protein docking and molecular dynamics Simulations. Analysis of docked complexes suggested that there are common insulin receptor residues for insulin and amyloid β binding. Further molecular dynamics Simulations study reveals that the monomeric form of amyloid β interacts with a similar set of receptor residues as observed in the insulin-insulin receptor complex.