Binding of levobupivacaine‐loaded gold nanoparticles to human serum albumin: a simulated physiological study

Abstract Techniques such as Fourier transform infrared (FTIR), ultraviolet–visible (UV–vis) spectra, fluorescence, circular dichroism (CD) and spectroscopy were applied to elucidate the formation, structure and physicochemical properties of levobupivacaine–gold nanoparticle (LGN) binding to human serum albumin (HSA). Thermodynamic parameters (Δ G = −2.58 × 10 4 J·mol −1 , Δ S = −7.80 J·mol −1 ·K −1 , and Δ S = −2.82 × 10 4 J·mol −1 at 305 K) suggested one weak binding site on HSA, which was governed by van der Waals forces as well as hydrogen bonds. Moreover, the outcomes of UV–vis, CD, FTIR, synchronous and three‐dimensional fluorescence suggested that the microenvironment of HSA had been changed with addition of LGN. Based on the results of fluorescence resonance energy transfer, a distance of 2.8 nm between the LGN and HSA was observed. This approach has potential value for illustrating the pharmacodynamics of LGN when in combination with transmembrane transport, biomolecular function effect, and other experiments.