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Risperidone (RIS), a widely used antipsychotic drug has pitfalls such as it is practically insoluble in water, it has an unpleasant taste, and exhibits photoinstability. Complex formation with milk protein, β-Lactoglobulin (β-LG) is a promising approach which could improve formulation of RIS. The current research work involves the study of the interactions of RIS with β-LG employing fluorimetry and molecular modelling. Fluorimetry was used to study stability of the complex of RIS with β-LG. This was supported with molecular modelling studies using induced fit docking (IFD), Molecular Mechanics-Generalized Born Surface Area (MMGBSA) and molecular dynamic (MD) simulation, to predict the binding mode, affinity and stability of the complex of RIS with β-LG. These studies indicated that RIS forms a stable complex with β-LG, mainly due to hydrophobic bonding which can be used for effective formulation of RIS.