Human Transferrin is a biochemical marker of iron status in the body. Transferrin (TF) is responsible for the transport of iron through the blood to various tissues. It is a blood plasma glycoprotein that plays a central role in iron metabolism. Members of the transferrin family are mostly monomeric glycoproteins, consisting of two lobes capable of binding ferric ions. When the binding sites are empty, transferrin is called apo-transferrin, as opposed to holo-transferrin, when the binding sites are occupied. The aim of this work is to determine the binding constant, number of binding sites and the binding mechanism between Olanzapine (OLZ) and TF by spectroscopic methods (fluorescence and absorption measurements). Results showed that Olanzapine reacts with transferrin and forms a TF-OLZ complex. The binding of olanzapine to transferrin is a spontaneous process. According to the calculated quenching constants, it appears that the quenching mechanism, which involves the formation of a complex, was found to be static. The main interactions between olanzapine and transferrin are hydrogen bonding and weak van der Waals forces.