Degradation of Human Serum Albumin by Infrared Free Electron Laser Enhanced by Inclusion of a Salen-Type Schiff Base Zn (II) Complex
dc.contributor.author | Onami, Yuika | |
dc.contributor.author | Kawasaki, Takayasu | |
dc.contributor.author | Aizawa, Hiroki | |
dc.contributor.author | Haraguchi, Tomoyuki | |
dc.contributor.author | Akitsu, Takashiro | |
dc.contributor.author | Tsukiyama, Koichi | |
dc.contributor.author | Alcolea Palafox, Mauricio | |
dc.date.accessioned | 2023-06-17T09:08:12Z | |
dc.date.available | 2023-06-17T09:08:12Z | |
dc.date.issued | 2020-01-29 | |
dc.description.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. | |
dc.description.department | Depto. de Química Física | |
dc.description.faculty | Fac. de Ciencias Químicas | |
dc.description.refereed | TRUE | |
dc.description.status | pub | |
dc.eprint.id | https://eprints.ucm.es/id/eprint/66279 | |
dc.identifier.doi | 10.3390/ijms21030874 | |
dc.identifier.issn | 1422-0067 | |
dc.identifier.officialurl | https://doi.org/10.3390/ijms21030874 | |
dc.identifier.relatedurl | https://www.mdpi.com/1422-0067/21/3/874 | |
dc.identifier.uri | https://hdl.handle.net/20.500.14352/8250 | |
dc.issue.number | 3 | |
dc.journal.title | International Journal of Molecular Sciences | |
dc.language.iso | eng | |
dc.page.initial | 874 | |
dc.publisher | MDPI | |
dc.rights | Atribución 3.0 España | |
dc.rights.accessRights | open access | |
dc.rights.uri | https://creativecommons.org/licenses/by/3.0/es/ | |
dc.subject.keyword | IR-FEL | |
dc.subject.keyword | human serum albumin | |
dc.subject.keyword | Schiff base | |
dc.subject.keyword | Zn(II) complex | |
dc.subject.keyword | TD-DFT | |
dc.subject.keyword | fluorescence | |
dc.subject.ucm | Química física (Química) | |
dc.title | Degradation of Human Serum Albumin by Infrared Free Electron Laser Enhanced by Inclusion of a Salen-Type Schiff Base Zn (II) Complex | |
dc.type | journal article | |
dc.volume.number | 21 | |
dspace.entity.type | Publication | |
relation.isAuthorOfPublication | 1163c7a4-e779-417f-867c-a6e963e4525e | |
relation.isAuthorOfPublication.latestForDiscovery | 1163c7a4-e779-417f-867c-a6e963e4525e |
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