Lurasidone hydrochloride is a second-generation (atypical) antipsychotic agent who is used for the treatment of schizophrenia and bipolar depression. The mechanism of action of lurasidone is not completely elucidated, assumed to affect dopamine and serotonin receptors, but is devoid of antihistaminic or anticholinergic activities [1].

Human serum albumin (HSA), the most abundant transport protein in blood plasma, consisting of 585 aminoacids residues and have three binding sites (I, II and III) [2,3]. The most of drugs binds to hydrophobic cavities in subdomains IIA and IIIA, in the site I and II, respetively. Investigation the interactions of drugs to HSA may give useful informations of effectiveness of drugs.

In this study, we investigate interactions between lurasidone and human serum albumin (HSA) by the fluorescence quenching technique, synchronous fluorescence spectroscopy and molecular docking.