LETTER TO THE EDITOR Spectroscopic and molecular docking approaches for the investigation of molecular interactions between herbicide sulfosulfuron and bovine serum albumin

摘要

1. Introduction Serum albumins are provided with manifold biological and pharmacokinetic functions, they can carry large variety of endogenous and exogenous compounds, such as nutrients, metabolites, fatty acids and a variety of phar-maceuticals to specific targets and serve as the container for the interacting bioactive substance. Among serum albumins, human serum albumin (HSA) and bovine serum albumin (BSA) are extensively studied as a model albumin in life sciences, chemistry, and clinical medicine. Both HSA and BSA display approximately 80% sequence homology and the tertiary structure of them is up to 76% (Naveenraj & Anandan, 2013). They are composed of three domains I, II, and III. Each domain has A and B sub-domains, forming a hydrophobic cavity. Hence, BSA is an idea model for evaluating the binding interaction of ligand with serum albumin due to its structural similarity with HSA, low cost, ready availability, and affordability (Elzoghby, Samy, & Elgindy, 2012). BSA consists of 583 amino acids with 20 tyrosyl (Tyr) residues and two tryptophan (Trpl34, Trp213) residues and there are 17 disulfide bonds which connect the individual helices, containing the two most active drug binding sites widely known as site I and site II (subdomain IIA and subdomain IIIA, respectively) (Supplementary Figure SI A).