The study investigates how the herbicide 2,4-D binds to human serum albumin (HSA) using various spectroscopic and computational techniques.
The formation of the 2,4-D-HSA complex was confirmed, revealing a weak binding affinity and identifying hydrophobic, van der Waals, and hydrogen bond interactions as key factors in the binding process.
Structural changes in HSA and improved thermal stability upon 2,4-D binding were also observed, with findings suggesting that the herbicide primarily binds at Sudlow's site I on the protein.