RT Journal Article
T1 Degradation of Human Serum Albumin by Infrared Free Electron Laser Enhanced by Inclusion of a Salen-Type Schiff Base Zn (II) Complex
A1 Onami, Yuika
A1 Kawasaki, Takayasu
A1 Aizawa, Hiroki
A1 Haraguchi, Tomoyuki
A1 Akitsu, Takashiro
A1 Tsukiyama, Koichi
A1 Alcolea Palafox, Mauricio
AB A salen-type Schiff base Zn(II) complex included in human serum albumin (HSA) protein was examined by UV-Vis, circular dichroism (CD), and fluorescence (PL) spectra. The formation of the composite material was also estimated by a GOLD program of ligand–protein docking simulation. A composite cast film of HSA and Zn(II) complex was prepared, and the effects of the docking of the metal complex on the degradation of protein molecules by mid-infrared free electron laser (IR-FEL) were investigated. The optimum wavelengths of IR-FEL irradiation to be used were based on experimental FT-IR spectra and vibrational analysis. Using TD-DFT results with 6-31G(d,p) and B3LYP, the IR spectrum of Zn(II) complex could be reasonably assigned. The respective wavelengths were 1652 cm−1 (HSA amide I), 1537 cm−1 (HSA amide II), and 1622 cm−1 (Zn(II) complex C=N). Degradation of HSA based on FT-IR microscope (IRM) analysis and protein secondary structure analysis program (IR-SSE) revealed that the composite material was degraded more than pure HSA or Zn(II) complex; the inclusion of Zn(II) complex enhanced destabilization of folding of HSA.
PB MDPI
SN 1422-0067
YR 2020
FD 2020-01-29
LK https://hdl.handle.net/20.500.14352/8250
UL https://hdl.handle.net/20.500.14352/8250
LA eng
DS Docta Complutense
RD 1 sept 2024