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

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 dipepti...

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Bibliographic Details
Published in:	International journal of molecular sciences Vol. 20; no. 11; p. 2846
Main Authors:	Onami, Yuika, Koya, Ryousuke, Kawasaki, Takayasu, Aizawa, Hiroki, Nakagame, Ryo, Miyagawa, Yoshito, Haraguchi, Tomoyuki, Akitsu, Takashiro, Tsukiyama, Koichi, Palafox, Mauricio A
Format:	Journal Article
Language:	English
Published:	Switzerland MDPI AG 11-06-2019 MDPI
Subjects:	Alanine Albumin amino acid derivative Amino acids Banded structure Circular dichroism Density functional theory Dichroism Excitation Free electron lasers Human serum albumin Humans I.R. radiation Imines Infrared lasers Infrared Rays Infrared spectroscopy IR-FEL Irradiation Lasers Light Proteins Schiff base Schiff Bases - chemistry Serum albumin Serum Albumin, Human - chemistry TD-DFT Ultraviolet radiation Valine Zinc - chemistry Zinc oxides Zn(II) complex Japan Schiff base IR-FEL human serum albumin Zn(II) complex amino acid derivative TD-DFT
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Summary:	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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1422-0067 1661-6596 1422-0067
DOI:	10.3390/ijms20112846