Premium
Binding of levobupivacaine‐loaded gold nanoparticles to human serum albumin: a simulated physiological study
Author(s) -
Cui Yanhong
Publication year - 2020
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.3888
Subject(s) - human serum albumin , chemistry , fourier transform infrared spectroscopy , van der waals force , hydrogen bond , fluorescence , circular dichroism , nanoparticle , protein secondary structure , analytical chemistry (journal) , biophysics , crystallography , molecule , nanotechnology , chromatography , materials science , organic chemistry , biochemistry , chemical engineering , physics , quantum mechanics , engineering , biology
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.