Evaluation of enantioselective binding of propanocaine to human serum albumin by ultrafiltration and electrokinetic chromatography under intermediate precision conditions

Martínez-Gómez, María Amparo; Escuder-Gilabert, Laura; Villanueva-Camañas, R.M.; Sagrado, S.; Medina-Hernández, M.J.

doi:10.1016/j.jchromb.2012.01.034

Cited by 4 publications

(1 citation statement)

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“…In order to study whether curcumin can replace the α-ZOL from HSA to form the HSA-curcumin complex, instead of forming an HSA-α-ZOL-curcumin complex, an ultrafiltration experiment was carried out. After the equilibration (incubation) of curcumin with HSA-α-ZOL mixtures according to Section 5.4, we separated the free α-ZOL (unbound fraction) and the HSA-α-ZOL complex (bound fraction) by ultrafiltration [28]. Therefore, the concentration of α-ZOL in the free state was examined by HPLC to confirm whether curcumin was able to displace α-ZOL from HSA, increasing the rate of α-ZOL in filtrate.…”

Section: Effect Of Curcumin On α-Zol-hsa Interactionmentioning

confidence: 99%

Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy

Tan

Zhou

et al. 2022

Toxins

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α-zearalenol (α-ZOL) is a mycotoxin with a strong estrogen effect that affects the synthesis and secretion of sex hormones and is transported to target organs through human serum albumin (HSA). Additionally, it has been reported that curcumin can also bind to HSA with high affinity at the same binding site as α-ZOL. Additionally, several studies reported that reducing the bound fraction of α-ZOL contributes to speeding up the elimination rate of α-ZOL to reduce its hazard to organs. Therefore, to explore the influence of a nutrition intervention with curcumin on α-ZOL effects, the competitive displacement of α-ZOL from HSA by curcumin was investigated using spectroscopic techniques, ultrafiltration techniques and HPLC methods. Results show that curcumin and α-ZOL share the same binding site (subdomain IIA) on HSA, and curcumin binds to HSA with a binding constant of 1.12 × 105 M−1, which is higher than that of α-ZOL (3.98 × 104 M−1). Ultrafiltration studies demonstrated that curcumin could displace α-ZOL from HSA to reduce α-ZOL’s binding fraction. Synchronous fluorescence spectroscopy revealed that curcumin could reduce the hydrophobicity of the microenvironment of an HSA–α-ZOL complex. This study is of great significance for applying curcumin and other highly active foodborne components to interfere with the toxicokinetics of α-ZOL and reduce its risk of its exposure.

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Section: Effect Of Curcumin On α-Zol-hsa Interactionmentioning

confidence: 99%