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 (ΔG = −2.58 × 10⁴ J·mol⁻¹, ΔS = −7.80 J·mol⁻¹·K⁻¹, and ΔS = −2.82 × 10⁴ 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.

中文翻译：

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左旋布比卡因负载金纳米颗粒与人血清白蛋白的结合：模拟生理研究。

诸如傅立叶变换红外（FTIR），紫外-可见（UV-vis）光谱，荧光，圆二色性（CD）和光谱学等技术被用来阐明左旋布比卡因-金纳米颗粒（LGN）与之结合的形成，结构和理化性质。人血清白蛋白（HSA）。热力学参数（ΔG = -2.58×10 ⁴ J·mol ^-1，ΔS = -7.80 J·mol ^-1 ·K ^-1，ΔS = -2.82×10 ⁴ J·mol ^-1在305 K）表明HSA上的一个弱结合位点是由范德华力以及氢键控制的。此外，UV-vis，CD，FTIR，同步和三维荧光的结果表明，添加LGN改变了HSA的微环境。基于荧光共振能量转移的结果，观察到LGN与HSA之间的距离为2.8nm。当与跨膜转运，生物分子功能效应和其他实验结合使用时，该方法具有说明LGN药效学的潜在价值。