Virtual Screening of Milk Proteins of Risperidone for Taste Improvement; Experimental Validation of Sodium Caseinate Binding by Fluorometry and Taste Assessment by Palatability Check Access

Risperidone (RIS), a widely used antipsychotic drug has patient’s non-compliance because of bitter taste. Taste improvement on the basis of milk proteins which seems likely to be effective due to their bio-compatibility, biodegradability, and also has several health benefits. The current research work encompasses the study of the binding interactions of RIS with milk protein employing molecular modelling and fluorometry. Molecular docking was performed for screening various milk proteins for their interactions of RIS with β-Lactoglobulin (β-LG), α-lactalbumin, lactoferrin, and casein which structure has not yet been elucidated by the X-ray crystallography or NMR spectroscopy so homology model of casein was constructed and validated using Ramachandran plot. RIS docked on these milk proteins and casein was found to be an effective mode of binding with RIS. induced fit docking, the Molecular Mechanics‐Generalized Born Surface Area were conducted for prediction of binding mode, along with binding affinity of RIS with casein and it was found effective mode of binding with RIS with casein. The fluorometry was used to study stability of the complex of RIS with NaCAS (sodium salt of casein). Bitter taste improvement potential of NaCAS with RIS was confirmed in-vivo using previously reported single bottle-test rat model. The NaCAS reduced RIS bitter perception, which could directly relate to its binding capacity. Thus Complex formation RIS with NaCAS is a promising approach for taste improvement of RIS.