Synergistic effects of metal-induced aggregation of human serum albumin
Synergistic effects of metal-induced aggregation of human serum albumin
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DOI：
10.1016/j.colsurfb.2018.10.061
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发表时间：
2019-01-01
影响因子：
5.8
通讯作者：
Lendel, Christofer
中科院分区：
文献类型：
--
作者：
Hedberg, Yolanda S.;Dobryden, Illia;Lendel, Christofer
钴（Co）、铬（Cr）和镍（Ni）的暴露通常通过皮肤接触以及不同的牙科和骨科植入物发生。金属离子与蛋白质结合，这可能引起结构变化和聚集，具有不同的医学后果。我们通过使用散射、光谱和成像技术，在模拟生理条件（磷酸盐缓冲盐水- PBS，pH 7.3）下，使用不影响pH的金属盐，并且在HSA：金属摩尔比高达1：8的条件下，研究了在Co-II、Cr-III和/或Ni-II离子和/或其纳米颗粒沉淀物存在下的人血清白蛋白（HSA）聚集。通过纳米颗粒追踪分析确定，在研究条件下，Co离子在PBS中形成了一些固体纳米颗粒，但Cr-III阴离子和Ni-II离子仍然完全溶解。结果发现，所有的金属离子诱导HSA聚集，并且当存在所有三种金属离子的混合物而不是任何单一类型的离子时，这种效果显著增强。因此，金属离子协同诱导聚集。在Cr-III离子存在下，HSA聚集体在云母表面形成线性结构。在所有三种金属离子的存在下，可以看到明显的聚集趋势和线性排列的聚集体。光谱研究表明，大多数的HSA分子保持其α螺旋二级结构和构象。本研究强调了金属离子和/或其沉淀物对蛋白质聚集的协同效应的重要性，这与植入材料和常见的金属暴露高度相关。
Exposure to cobalt (Co), chromium (Cr), and nickel (Ni) occurs often via skin contact and from different dental and orthopedic implants. The metal ions bind to proteins, which may induce structural changes and aggregation, with different medical consequences. We investigated human serum albumin (HSA) aggregation in the presence of Co-II, Cr-III, and/or Ni-II ions and/or their nanoparticle precipitates by using scattering, spectroscopic, and imaging techniques, at simulated physiological conditions (phosphate buffered saline - PBS, pH 7.3) using metal salts that did not affect the pH, and at HSA:metal molar ratios of up to 1:8. Co ions formed some solid nano particles in PBS at the investigated conditions, as determined by nanoparticle tracking analysis, but the Cr-III anions and Ni-II ions remained fully soluble. It was found that all metal ions induced HSA aggregation, and this effect was significantly enhanced when a mixture of all three metal ions was present instead of any single type of ion. Thus, the metal ions induce aggregation synergistically. HSA aggregates formed linear structures on a mica surface in the presence of Cr-III ions. A clear tendency of aggregation and linearly aligned aggregates was seen in the presence of all three metal ions. Spectroscopic investigations indicated that the majority of the HSA molecules maintained their alpha helical secondary structure and conformation. This study highlights the importance of synergistic effects of metal ions and/or their precipitates on protein aggregation, which are highly relevant for implant materials and common exposures to metals.