Investigation by DFT methods of the damage of human serum albumin including amino acid derivative schiff base Zn(II) complexes by IR-FEL irradiation

Yuika Onami, Ryousuke Koya, Takayasu Kawasaki, Hiroki Aizawa, Ryo Nakagame, Yoshito Miyagawa, Tomoyuki Haraguchi, Takashiro Akitsu, Koichi Tsukiyama, Mauricio A. Palafox

研究成果: Article査読

4 被引用数 (Scopus)

抄録

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.

本文言語English
論文番号2846
ジャーナルInternational journal of molecular sciences
20
11
DOI
出版ステータスPublished - 1 6月 2019

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