Investigation by DFT Methods of the Damage of Human Serum Albumin Including Amino Acid Derivative Schiff Base Zn(II) Complexes by IR-FEL Irradiation

International Journal of Molecular Sciences

MauricioA. Palafox¹  Tomoyuki Haraguchi²  Hiroki Aizawa²  Yuika Onami²  Ryousuke Koya²  Ryo Nakagame²  Takashiro Akitsu²  Koichi Tsukiyama²  Yoshito Miyagawa²  Takayasu Kawasaki³ 

[1] Departamento de Química-Física, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, Madrid-28040, Spain;Department of Chemistry, Faculty of Science, Tokyo University of Science, 1-3 Kagurazaka, Shinjuku-ku, Tokyo 162-8601, Japan;FEL-TUS, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan;

关键词: TD-DFT;    IR-FEL;    human serum albumin;    amino acid derivative;    Schiff base;    Zn(II) complex;   

DOI  :  10.3390/ijms20112846

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown