Alzheimer's disease is a type of brain dysfunction that gradually degrades the memory of the senile. The aggregation of beta-amyloid peptide (1-42) is considered to be closely related to Alzheimer's disease. Betaamyloid peptide (1-42) is neurotoxic and characterized by fast aggregation. During the aggregation, a conformational change has been identified, whereby a salt bridge is formed between Lys28 and Asp23 or Glu22. Hence in this study, a pharmacophore model was constructed from beta-amyloid inhibitor (curcumin), virtual screened compounds from the ten databases. 120 compounds showed good agreement with the pharmaccophore model and 14 of these compounds obey the linspinsky rule. The molecular docking studies were done to examine the interactions among beta-amyloid peptide (1-42) with screened substances. Compound CSC090985722 had the lowest bond energy (-19.68 kJ/mol) according to the molecular docking results. The important hydrogen bond interactions were observed between screened compounds with Glu22, Asp23, or loops 10–33 which are located at the binding site