RT Journal Article
T1 Investigation by DFT Methods of the Damage of Human Serum Albumin Including Amino Acid Derivative Schiff Base Zn(II) Complexes by IR-FEL Irradiation
A1 Onami, Yuika
A1 Koya, Ryousuke
A1 Kawasaki, Takayasu
A1 Aizawa, Hiroki
A1 Nakagame, Ryo
A1 Miyagawa, Yoshito
A1 Haraguchi, Tomoyuki
A1 Akitsu, Takashiro
A1 Tsukiyama, Koichi
A1 Alcolea Palafox, Mauricio
AB 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.
PB MDPI
SN 1422-0067
YR 2019
FD 2019-06-11
LK https://hdl.handle.net/20.500.14352/12606
UL https://hdl.handle.net/20.500.14352/12606
LA eng
DS Docta Complutense
RD 1 sept 2024