Onami, YuikaKoya, RyousukeKawasaki, TakayasuAizawa, HirokiNakagame, RyoMiyagawa, YoshitoHaraguchi, TomoyukiAkitsu, TakashiroTsukiyama, KoichiAlcolea Palafox, Mauricio2023-06-172023-06-172019-06-111422-006710.3390/ijms20112846https://hdl.handle.net/20.500.14352/12606An 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.engAtribución 3.0 Españajournal articlehttps://doi.org/10.3390/ijms20112846https://www.mdpi.com/1422-0067/20/11/2846open accessTD-DFTIR-FELhuman serum albuminamino acid derivativeSchiff baseZn(II) complexQuímica física (Química)