L. R. Bogdanova, A. A. Nikiforova, S. A. Ziganshina, Yu. F. Zuev, I. A. Sedov
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引用次数: 0
Abstract
The effect of binding of divalent metal cations (Ca2+, Cu2+, Mg2+, Mn2+, Zn2+) on the kinetics of fibril formation of bovine α-lactalbumin at acidic conditions is considered. The kinetic parameters of the process were determined using a thioflavin T fluorescence assay. The DSC thermograms of bovine α-lactalbumin in the presence and absence of cations were recorded. The duration of the lag period correlates with the changes in the thermal stability of the molten globule of the protein in the presence of cations. The final thioflavin T fluorescence intensity after formation of the mature fibrils decreases under the influence of calcium ions which strongly bind to the monomeric protein, and increases in solutions containing copper and especially zinc. These ions seem to accelerate secondary nucleation processes and change the fibril morphology, which was confirmed by atomic force microscopy imaging.
研究考虑了二价金属阳离子（Ca2+、Cu2+、Mg2+、Mn2+、Zn2+）的结合对酸性条件下牛α-乳白蛋白纤维形成动力学的影响。使用硫黄素 T 荧光测定法确定了这一过程的动力学参数。记录了存在和不存在阳离子时牛 α-乳白蛋白的 DSC 热图。滞后期的长短与存在阳离子时蛋白质熔融球的热稳定性变化相关。成熟纤维形成后，最终的硫黄素 T 荧光强度在钙离子的影响下会降低，因为钙离子会与单体蛋白质紧密结合，而在含铜（尤其是锌）的溶液中则会升高。这些离子似乎加速了二次成核过程并改变了纤维的形态，原子力显微镜成像证实了这一点。
期刊介绍：
Biological inorganic chemistry is a growing field of science that embraces the principles of biology and inorganic chemistry and impacts other fields ranging from medicine to the environment. JBIC (Journal of Biological Inorganic Chemistry) seeks to promote this field internationally. The Journal is primarily concerned with advances in understanding the role of metal ions within a biological matrix—be it a protein, DNA/RNA, or a cell, as well as appropriate model studies. Manuscripts describing high-quality original research on the above topics in English are invited for submission to this Journal. The Journal publishes original articles, minireviews, and commentaries on debated issues.
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