Application of Infrared Free-Electron Laser Irradiation of Protein Complexes Binding to Salen-Type Schiff Base Zn(II) Complexes Using Secondary Conformational Changes in the Proteins for the Treatment of Alzheimer’s Disease
Alzheimer’s disease causes the destruction of cranial nerve cells and is said to be caused by neuronal cell death due to the accumulation of amyloid-β protein. One method for the treatment of Alzheimer’s disease is to reduce the toxicity of the amyloid beta protein. Among the possibilities is to red...
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| Format: | Article |
| Language: | English |
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MDPI AG
2024-02-01
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| Series: | Inorganics |
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| Online Access: | https://www.mdpi.com/2304-6740/12/2/50 |
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| author | Hiroshi Takashima Daisuke Nakane Takashiro Akitsu |
| author_facet | Hiroshi Takashima Daisuke Nakane Takashiro Akitsu |
| author_sort | Hiroshi Takashima |
| collection | DOAJ |
| description | Alzheimer’s disease causes the destruction of cranial nerve cells and is said to be caused by neuronal cell death due to the accumulation of amyloid-β protein. One method for the treatment of Alzheimer’s disease is to reduce the toxicity of the amyloid beta protein. Among the possibilities is to reduce toxicity by changing the secondary structure of the protein. In this study, the secondary structure of the protein was verified by binding a zinc complex to the protein and irradiating it with an infrared free-electron laser (IR-FEL). By binding Salen-Type zinc complexes to human serum albumin (HSA) and irradiating it with IR-FEL, structural changes were observed in the α-helix and β-sheet, the secondary structure of HSA. In addition to researching the possibility of binding zinc complexes to small proteins, docking simulations were examined. GOLD docking simulations showed that it is possible to bind zinc complexes to lysozyme (Lyz), a small protein. These results suggest that binding zinc complexes to amyloid-β and inducing a secondary conformational change through IR-FEL irradiation could be used for the treatment of Alzheimer’s disease by making the complexes lose their toxicity. |
| first_indexed | 2024-03-07T22:27:39Z |
| format | Article |
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| institution | Directory Open Access Journal |
| issn | 2304-6740 |
| language | English |
| last_indexed | 2024-03-07T22:27:39Z |
| publishDate | 2024-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Inorganics |
| spelling | doaj.art-6af29f0dd0a14278b5dc9bd8fb55dd6e2024-02-23T15:21:20ZengMDPI AGInorganics2304-67402024-02-011225010.3390/inorganics12020050Application of Infrared Free-Electron Laser Irradiation of Protein Complexes Binding to Salen-Type Schiff Base Zn(II) Complexes Using Secondary Conformational Changes in the Proteins for the Treatment of Alzheimer’s DiseaseHiroshi Takashima0Daisuke Nakane1Takashiro Akitsu2Department of Chemistry, Faculty of Science, Tokyo University of Science, 1-3 Kagurazaka, Tokyo 162-8601, JapanDepartment of Chemistry, Faculty of Science, Tokyo University of Science, 1-3 Kagurazaka, Tokyo 162-8601, JapanDepartment of Chemistry, Faculty of Science, Tokyo University of Science, 1-3 Kagurazaka, Tokyo 162-8601, JapanAlzheimer’s disease causes the destruction of cranial nerve cells and is said to be caused by neuronal cell death due to the accumulation of amyloid-β protein. One method for the treatment of Alzheimer’s disease is to reduce the toxicity of the amyloid beta protein. Among the possibilities is to reduce toxicity by changing the secondary structure of the protein. In this study, the secondary structure of the protein was verified by binding a zinc complex to the protein and irradiating it with an infrared free-electron laser (IR-FEL). By binding Salen-Type zinc complexes to human serum albumin (HSA) and irradiating it with IR-FEL, structural changes were observed in the α-helix and β-sheet, the secondary structure of HSA. In addition to researching the possibility of binding zinc complexes to small proteins, docking simulations were examined. GOLD docking simulations showed that it is possible to bind zinc complexes to lysozyme (Lyz), a small protein. These results suggest that binding zinc complexes to amyloid-β and inducing a secondary conformational change through IR-FEL irradiation could be used for the treatment of Alzheimer’s disease by making the complexes lose their toxicity.https://www.mdpi.com/2304-6740/12/2/50IR-FELcomplexamyloid-βHSAzincsecondary structure |
| spellingShingle | Hiroshi Takashima Daisuke Nakane Takashiro Akitsu Application of Infrared Free-Electron Laser Irradiation of Protein Complexes Binding to Salen-Type Schiff Base Zn(II) Complexes Using Secondary Conformational Changes in the Proteins for the Treatment of Alzheimer’s Disease Inorganics IR-FEL complex amyloid-β HSA zinc secondary structure |
| title | Application of Infrared Free-Electron Laser Irradiation of Protein Complexes Binding to Salen-Type Schiff Base Zn(II) Complexes Using Secondary Conformational Changes in the Proteins for the Treatment of Alzheimer’s Disease |
| title_full | Application of Infrared Free-Electron Laser Irradiation of Protein Complexes Binding to Salen-Type Schiff Base Zn(II) Complexes Using Secondary Conformational Changes in the Proteins for the Treatment of Alzheimer’s Disease |
| title_fullStr | Application of Infrared Free-Electron Laser Irradiation of Protein Complexes Binding to Salen-Type Schiff Base Zn(II) Complexes Using Secondary Conformational Changes in the Proteins for the Treatment of Alzheimer’s Disease |
| title_full_unstemmed | Application of Infrared Free-Electron Laser Irradiation of Protein Complexes Binding to Salen-Type Schiff Base Zn(II) Complexes Using Secondary Conformational Changes in the Proteins for the Treatment of Alzheimer’s Disease |
| title_short | Application of Infrared Free-Electron Laser Irradiation of Protein Complexes Binding to Salen-Type Schiff Base Zn(II) Complexes Using Secondary Conformational Changes in the Proteins for the Treatment of Alzheimer’s Disease |
| title_sort | application of infrared free electron laser irradiation of protein complexes binding to salen type schiff base zn ii complexes using secondary conformational changes in the proteins for the treatment of alzheimer s disease |
| topic | IR-FEL complex amyloid-β HSA zinc secondary structure |
| url | https://www.mdpi.com/2304-6740/12/2/50 |
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