Interaction of glycated myoglobin with trifluoperazine: A biophysical elucidation of the consequences

Abstract

Affinity of a protein towards a drug depends on its structural configuration. High concentration of glucose as occurred in diabetes mellitus interacts with proteins and other molecules. Glycation of protein interferes the structure, resulting modification in its interaction profile with drugs. Trifluoperazine (TFZ), a phenothiazine group of drugs is used widely for the treatment of psychopathy. It is reported that interaction of TFZ with hemoglobin is largely affected by the glycation of the later. Myoglobin (Mb), another heme protein is identical to hemoglobin in many respects and comes out of the muscle to the blood stream during vigorous exercise. As a result, myoglobin also gets glycated in diabetic patients. However, the interaction profile of TFZ-Mb upon glycation has not been established yet. With this view, here a comparative study on the interaction of TFZ with Mb and glycated myoglobin (GMb) is reported. The study is purely based on spectrofluorimetric analysis. The binding parameters like, binding affinity constant and binding sites as well as the nature of the interactions are studied. It is concluded that the affinity of myoglobin is significantly increased upon glycation, however, the number of binding sites and the nature of interaction remain unaffected.