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Binding of vanadium to human serum transferrin - voltammetric and spectrometric studies
Journal of Inorganic Biochemistry ( IF 3.9 ) Pub Date : 2017-12-26 , DOI: 10.1016/j.jinorgbio.2017.12.012
Cristina G. Azevedo , Isabel Correia , Margarida M.C. dos Santos , Marino F.A. Santos , Teresa Santos-Silva , James Doutch , Luz Fernandes , Hugo M. Santos , José L. Capelo , João Costa Pessoa

Previous studies generally agree that in the blood serum vanadium is transported mainly by human serum transferrin (hTF). In this work through the combined use of electrochemical techniques, matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) mass spectrometry and small-angle X-ray scattering (SAXS) data it is confirmed that both VIV and VV bind to apo-hTF and holo-hTF. The electrochemical behavior of solutions containing vanadate(V) solutions at pH = 7.0, analyzed by using two different voltammetric techniques, with different time windows, at a mercury electrode, Differential Pulse Polarography (DPP) and Cyclic Voltammetry (CV), is consistent with a stepwise reduction of VV → VIV and VIV → VII. Globally the voltammetric data are consistent with the formation of 2:1 complexes in the case of the system VV-apo-hTF and both 1:1 and 2:1 complexes in the case of VV-holo-hTF; the corresponding conditional formation constants were estimated. MALDI-TOF mass spectrometric data carried out with samples of VIVOSO4 and apo-hTF and of NH4VVO3 with both apo-hTF and holo-hTF with V:hTF ratios of 3:1 are consistent with the binding of vanadium to the proteins. Additionally the SAXS data suggest that both VIVOSO4 and NaVVO3 can effectively interact with human apo-transferrin, but for holo-hTF no clear evidence was obtained supporting the existence or the absence of protein-ligand interactions. This latter data suggest that the conformation of holo-hTF does not change in the presence of either VIVOSO4 or NH4VVO3. Therefore, it is anticipated that VIV or VV bound to holo-hTF may be efficiently up-taken by the cells through receptor-mediated endocytosis of hTF.



中文翻译:

钒与人血清转铁蛋白的结合-伏安法和光谱法研究

先前的研究普遍认为,血清中的钒主要由人血清转铁蛋白(hTF)转运。在这项工作中,通过结合使用电化学技术,基质辅助激光解吸/电离飞行时间(MALDI-TOF)质谱和小角度X射线散射(SAXS)数据,可以确定V IV和V V绑定到apo-hTF和holo-hTF。通过使用两种不同的伏安技术,在不同时间窗口下,在汞电极上使用差动脉冲极谱法(DPP)和循环伏安法(CV)分析了含钒酸盐(V)溶液在pH = 7.0的溶液的电化学行为,与逐步降低V V  →V IV和V IV →V II。总体而言,伏安数据在系统V V -apo-hTF的情况下与2:1配合物的形成是一致的,在V V -holo-hTF的情况下与1:1和2:1配合物的形成是一致的。估计了相应的条件形成常数。V IV OSO 4和apo-hTF样品以及NH 4 V V O 3和apo-hTF和holo-hTF样品的V:hTF比为3:1的样品进行的MALDI-TOF质谱数据与结合一致钒对蛋白质的作用。此外,SAXS数据还表明V IV OSO 4和NaV V O 3可以有效地与人类载脂蛋白转铁蛋白相互作用,但对于hlo-hTF,没有获得明确的证据支持蛋白质-配体相互作用的存在或不存在。后一数据表明,在存在V IV OSO 4或NH 4 V V O 3的情况下,holo-hTF的构象不会改变。因此,可以预料,结合至完整hTF的V IV或V V可以通过受体介导的hTF内吞作用被细胞有效地摄取。

更新日期:2017-12-26
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