Onami, YuikaKawasaki, TakayasuAizawa, HirokiHaraguchi, TomoyukiAkitsu, TakashiroTsukiyama, KoichiAlcolea Palafox, Mauricio2023-06-172023-06-172020-01-291422-006710.3390/ijms21030874https://hdl.handle.net/20.500.14352/8250A 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.engAtribución 3.0 Españajournal articlehttps://doi.org/10.3390/ijms21030874https://www.mdpi.com/1422-0067/21/3/874open accessIR-FELhuman serum albuminSchiff baseZn(II) complexTD-DFTfluorescenceQuímica física (Química)