Other Biochemistry, Biophysics, and Structural Biology Commons^™

Investigating Quinclorac Binding To Human Serum Albumin Using Spectroscopy And Molecular Docking, Le Nguyen, L. Hicks, L. Jodoin, S. Carby, D. S. Sanford, D. Benavides, A. Mishra, R. Yadav

Journal of the Arkansas Academy of Science

Human serum albumin (HSA) is the most abundant plasma protein and serves as a major transporter and reservoir for a wide range of endogenous ligands, including fatty acids, heme, bilirubin, prostaglandins, and metal ions, as well as numerous exogenous compounds, such as pharmaceuticals. HSA is a 66 kDa monomeric, multidomain protein containing two principal ligand-binding sites, Sudlow sites I and II. Sudlow site I contains Trp214, the sole tryptophan residue in HSA, whose intrinsic fluorescence provides a sensitive probe for studying ligand–protein interactions.

In this study, the interaction between HSA and the persistent organochlorine herbicide quinclorac (QNC) was investigated using …

Human Serum Albumin Interaction With Organochlorine Pesticides, D. S. Sanford, R. Yadav, A. Mishra

Journal of the Arkansas Academy of Science

Human serum albumin (HSA) is the most abundant blood plasma protein and plays a crucial role in drug transport and physiological homeostasis. HSA has a highly flexible structure consisting of three domains, each with multiple binding sites lined with hydrophobic and hydrophilic residues. The structural properties of HSA make it a robust reservoir and receptor for various endogenous and exogenous compounds, including therapeutic drugs. Organochlorine pesticides (OCPs) are a subclass of pesticides characterized by their chlorine content. Once widely used, these compounds remain persistent in the environment and biological systems despite regulatory restrictions in many developed countries. The strong ligand-binding …