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

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

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.

Original languageEnglish
Article number2846
JournalInternational journal of molecular sciences
Volume20
Issue number11
DOIs
Publication statusPublished - 1 Jun 2019

Keywords

  • Amino acid derivative
  • Human serumalbumin
  • IR-FEL
  • Schiff base
  • TD-DFT
  • Zn(II) complex

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