Investigation by DFT Methods of the Damage of Human Serum Albumin Including Amino Acid Derivative Schiff Base Zn(II) Complexes by IR-FEL Irradiation
Investigation by DFT Methods of the Damage of Human Serum Albumin Including Amino Acid Derivative Schiff Base Zn(II) Complexes by IR-FEL Irradiation
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DOI：
10.3390/ijms20112846
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发表时间：
2019-06-01
影响因子：
5.6
通讯作者：
Palafox, Mauricio A.
中科院分区：
文献类型：
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作者：
Onami, Yuika;Koya, Ryousuke;Palafox, Mauricio A.
红外自由电子激光(IR-FEL)可以通过激发振动带来分解聚集的蛋白质。在本研究中，我们制备了蛋白质(人血清白蛋白)杂化材料，包括几个新的含有氨基酸(丙氨酸和缬氨酸)或二肽(甘氨酸-甘氨酸)衍生物的席夫碱锌(II)配合物，并用UV-Vis、圆二色谱(CD)和红外光谱对其进行了表征。用密度泛函理论(DFT)和含时密度泛函(TD-DFT)方法研究了锌(II)络合物的振动模式。用IR-FEL在亚胺C=N、酰胺I和酰胺II带对应的波长照射人血清白蛋白和人血清白蛋白-锌(II)络合物杂化材料。二级结构分析表明，在HSA中引入一个锌(II)络合物导致了HSA的结构变化，导致了比原来的HSA更脆弱的结构。这是红外自由电子激光振动激发不同于紫外光或可见光电子激发的特征之一。
An infrared free electron laser (IR-FEL) can decompose aggregated proteins by excitation of vibrational bands. In this study, we prepared hybrid materials of protein (human serum albumin; HSA) including several new Schiff base Zn(II) complexes incorporating amino acid (alanine and valine) or dipeptide (gly-gly) derivative moieties, which were synthesized and characterized with UV-vis, circular dichroism (CD), and IR spectra. Density functional theory (DFT) and time dependent DFT (TD-DFT) calculations were also performed to investigate vibrational modes of the Zn(II) complexes. An IR-FEL was used to irradiate HSA as well as hybrid materials of HSA-Zn(II) complexes at wavelengths corresponding to imine C=N, amide I, and amide II bands. Analysis of secondary structures suggested that including a Zn(II) complex into HSA led to the structural change of HSA, resulting in a more fragile structure than the original HSA. The result was one of the characteristic features of vibrational excitation of IR-FEL in contrast to electronic excitation by UV or visible light.