Degradation of Human Serum Albumin by Infrared Free Electron Laser Enhanced by Inclusion of a Salen-Type Schiff Base Zn (II) Complex

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Onami, Yuika and Kawasaki, Takayasu and Aizawa, Hiroki and Haraguchi, Tomoyuki and Akitsu, Takashiro and Tsukiyama, Koichi and Alcolea Palafox, Mauricio (2020) Degradation of Human Serum Albumin by Infrared Free Electron Laser Enhanced by Inclusion of a Salen-Type Schiff Base Zn (II) Complex. International Journal of Molecular Sciences, 21 (3). p. 874. ISSN 1422-0067

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Official URL: https://doi.org/10.3390/ijms21030874




Abstract

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.


Item Type:Article
Uncontrolled Keywords:IR-FEL; human serum albumin; Schiff base; Zn(II) complex; TD-DFT; fluorescence
Subjects:Sciences > Chemistry > Chemistry, Physical and theoretical
ID Code:66279
Deposited On:28 Jun 2021 15:10
Last Modified:07 Jul 2021 07:06

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