Evaluation of terbinafine interaction with human serum albumin by circular dichroism, capillary electrophoresis and spectroscopy

Abstract

Human serum albumin (HSA) is the most abundant protein in human plasma and constitutes about 60% of all proteins there. It is established as a versatile, non – specific transporter and plays a significant role in binding a wide variety of drugs that are delivered to their target tissues. The study about possible binding interactions between HSA and certain drugs can provide important information about medicine behavior in the human body and its pharmacokinetic characteristics [1]. Terbinafine is allylamine antifungal agent, which is well established for onychomycosis treatment. Considering the facts that terbinafine is widely used by administrating it orally, and that more than 99% of the dose can be bound to plasma proteins, the binding mechanisms and intensity are still studied [2]. The aim of this study was to investigate possible interaction between HSA and terbinafine applying circular dichroism (CD), capillary electrophoresis (CE), Fourier transform infrared spectroscopy (FT-IR) and ultraviolet and visible absorption (UV-vis) spectroscopy. Considering that terbinafine is a basic hydrophobic agent (pKa=8,94) and is very slightly soluble in water, the investigation was performed under conditions of pH=7,4 and pH=3, because solubility of terbinafine increasing in acidic water.[...]