Spectroscopic Characterization of the Interaction between Dopamine and Human Serum Albumin

Abstract

The interactions of HSA with DA have received great attention nowadays due to its significant effect in the biomedical field and overall health. The main aim of this work is to examine the interaction between DA and HSA at physiological conditions. Upon addition of DA to HSA, the fluorescence emission was quenched with quenching constant Kq = 1.32 × 109 L⋅mol−1⋅s−1 and the binding constant of DA with HSA is found to be K = 4.4 × 102 mainly indicating dynamic quenching. The HSA conformation was altered upon binding of DA to HSA with an increase in α-helix and a decrease in β-sheets suggesting unfolding of HSA secondary structure due to weak intermolecular interaction with HSA. In view of the evidence presented, it is important to understand the details of the interactions of HSA with DA which will be crucial in the design of new DA-inspired drugs and help revealing vital details to better understand the HSA’s role as a transporter for many drugs.