Characterizing N-acetylcysteine (NAC) and N-acetylcysteine Amide (NACA) Binding For Lead Poisoning Treatment
Using antioxidants is an important means of treating lead poisoning. Prior in vivo studies showed marked differences between various chelator antioxidants in their ability to decrease both blood Pb(II) levels and oxidative stress resulting from lead poisoning. The comparative abilities of NAC and NACA to Pb(II) were studied in vitro, for the first time, to examine the role of the single bondOH/single bondNH2 functional group in antioxidant binding behavior. To assay the antioxidant-divalent metal interaction, the antioxidants were probed as solid surfaces, adsorbing Pb(II) onto them. Surface characterization was carried out using X-ray photoelectron spectroscopy (XPS) analysis to quantify Pb(II) in the resulting adducts. XPS of the Pb 4f orbitals showed that more Pb(II) was chemically bound to NACA than NAC. In addition, the antioxidant surfaces probed via point-of-zero charge (PZC) measurements of NAC and NACA were obtained to gain further insight into the Pb-NAC and Pb-NACA binding, showing that Coulombic interactions played a partial role in facilitating complex formation. The data correlated well with solution analysis of metal-ligand complexation. UV-vis spectroscopy was used to probe complexation behavior. NACA was found to have the higher binding affinity as shown by free Pb(II) available in the solution after complexation from HPLC data. Electrospray ionization mass spectrometry (ESI-MS) was applied to delineate the structures of Pb-antioxidant complexes. Experimental results were further supported by density functional theory (DFT) calculations of supermolecular interaction energies (Einter) showing a greater interaction of Pb(II) with NACA than NAC.
N. Ercal et al., "Characterizing N-acetylcysteine (NAC) and N-acetylcysteine Amide (NACA) Binding For Lead Poisoning Treatment," Journal of Colloid and Interface Science, Elsevier, Apr 2012.
The definitive version is available at https://doi.org/10.1016/j.jcis.2011.12.052
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© 2012 Elsevier, All rights reserved.
01 Apr 2012