Interaction of Cuminaldehyde with Bovine Serum Albumin and Human Serum Albumin

Abstract

Abstract Cuminaldehyde, an oxidized aldehyde monoterpene, present in green cumin seeds (CuminumcyminumLinn,FamilyApiaceae), is traditionally used for the treatment of abdominal colic, dyspepsia , diarrhoea and jaundice. Also, many studies have reported the antioxidant, antibacterial and antifungal effects of Cuminaldehyde. Serum albumins are the major soluble and small molecule-binding proteins, present in abundance in the circulatory system of a wide variety of organisms. Studies on the interaction of bioactive molecules with Bovine serum albumin(BSA) and Human serum albumin(HSA) have attracted enormous interest due to its direct consequence on drug delivery, pharmacokinetics, pharmacodynamics, therapeutic efficacy and drug designing. Our present study is carried out to understand the mechanism of interaction of pharmaceutically important component of spices, Cuminaldehyde with BSA and HSA. Fluorescence spectroscopic measurements confirmed that Cuminaldehyde interacted with BSA and HSA and quenched its fluorescence intensity via static quenching mechanism. The change in secondary conformation of BSA and HSA upon interaction with Cuminaldehyde was explored by UV-Visible absorption studies. The location of binding site for Cuminaldehyde in BSA and HSA was investigated by site probe displacement experiments and the results indicated that Cuminaldehyde was bound to BSA and HSA at site I. Thermodynamic studies revealed that vander Waal’s interaction and hydrogen bonding play a major role in Cuminaldehyde-BSA system while electrostatic interaction plays vital role in Cuminaldehyde-HSA system.