Exploring EPR Parameters of 187Re Complexes for Designing New MRI Probes: From the Gas Phase to Solution and a Model Protein Environment
Breast cancer is one of the major types of cancer around the world, and early diagnosis is essential for successful treatment. New contrast agents (CAs), with reduced toxicology, are needed to improve diagnosis. One of the most promising Magnetic Resonance Imaging (MRI) CA is based on rhenium conjug...
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Wiley
2022-01-01
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| Series: | Journal of Chemistry |
| Online Access: | http://dx.doi.org/10.1155/2022/7056284 |
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| author | Gustavo A. Andolpho Elaine F. F. da Cunha Teodorico C. Ramalho |
| author_facet | Gustavo A. Andolpho Elaine F. F. da Cunha Teodorico C. Ramalho |
| author_sort | Gustavo A. Andolpho |
| collection | DOAJ |
| description | Breast cancer is one of the major types of cancer around the world, and early diagnosis is essential for successful treatment. New contrast agents (CAs), with reduced toxicology, are needed to improve diagnosis. One of the most promising Magnetic Resonance Imaging (MRI) CA is based on rhenium conjugated with a benzothiazole derivate (ReABT). In this sense, DFT has been used to evaluate the best methodology for calculating the hyperfine coupling constant (Aiso) of ReABT. Then, a thermodynamic analysis was performed to confirm the stability of the complex. Furthermore, a docking study of ReABT at the enzyme PI3K active site and Aiso calculations of ReABT in the enzyme environment were carried out. The best methodology for the Aiso calculation of ReABT was using the M06L functional, SARC-ZORA-TZVP (for Re) and TZVP (for all other atoms) basis set, relativistic Hamiltonian, and the CPCM solvation model with water as the solvent which confirm that the relativistic effects are important for calculating the Aiso values. In addition, thermodynamic analysis indicates that ReABT presents a higher stability and a lower toxicity than Gd-based CAs. The docking studies point out that ReABT interacts with amino acids residues of alanine, aspartate, and lysine from the PI3K active site. Considering the enzyme environment, Aiso values decrease significantly. These findings indicate that the CA candidate ReABT could be a good candidate for a new contrast agent. |
| format | Article |
| id | doaj-art-5bb7ec96850e429bb77e77837ee21196 |
| institution | Kabale University |
| issn | 2090-9071 |
| language | English |
| publishDate | 2022-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Chemistry |
| spelling | doaj-art-5bb7ec96850e429bb77e77837ee211962025-02-03T01:00:43ZengWileyJournal of Chemistry2090-90712022-01-01202210.1155/2022/7056284Exploring EPR Parameters of 187Re Complexes for Designing New MRI Probes: From the Gas Phase to Solution and a Model Protein EnvironmentGustavo A. Andolpho0Elaine F. F. da Cunha1Teodorico C. Ramalho2Chemistry DepartmentChemistry DepartmentChemistry DepartmentBreast cancer is one of the major types of cancer around the world, and early diagnosis is essential for successful treatment. New contrast agents (CAs), with reduced toxicology, are needed to improve diagnosis. One of the most promising Magnetic Resonance Imaging (MRI) CA is based on rhenium conjugated with a benzothiazole derivate (ReABT). In this sense, DFT has been used to evaluate the best methodology for calculating the hyperfine coupling constant (Aiso) of ReABT. Then, a thermodynamic analysis was performed to confirm the stability of the complex. Furthermore, a docking study of ReABT at the enzyme PI3K active site and Aiso calculations of ReABT in the enzyme environment were carried out. The best methodology for the Aiso calculation of ReABT was using the M06L functional, SARC-ZORA-TZVP (for Re) and TZVP (for all other atoms) basis set, relativistic Hamiltonian, and the CPCM solvation model with water as the solvent which confirm that the relativistic effects are important for calculating the Aiso values. In addition, thermodynamic analysis indicates that ReABT presents a higher stability and a lower toxicity than Gd-based CAs. The docking studies point out that ReABT interacts with amino acids residues of alanine, aspartate, and lysine from the PI3K active site. Considering the enzyme environment, Aiso values decrease significantly. These findings indicate that the CA candidate ReABT could be a good candidate for a new contrast agent.http://dx.doi.org/10.1155/2022/7056284 |
| spellingShingle | Gustavo A. Andolpho Elaine F. F. da Cunha Teodorico C. Ramalho Exploring EPR Parameters of 187Re Complexes for Designing New MRI Probes: From the Gas Phase to Solution and a Model Protein Environment Journal of Chemistry |
| title | Exploring EPR Parameters of 187Re Complexes for Designing New MRI Probes: From the Gas Phase to Solution and a Model Protein Environment |
| title_full | Exploring EPR Parameters of 187Re Complexes for Designing New MRI Probes: From the Gas Phase to Solution and a Model Protein Environment |
| title_fullStr | Exploring EPR Parameters of 187Re Complexes for Designing New MRI Probes: From the Gas Phase to Solution and a Model Protein Environment |
| title_full_unstemmed | Exploring EPR Parameters of 187Re Complexes for Designing New MRI Probes: From the Gas Phase to Solution and a Model Protein Environment |
| title_short | Exploring EPR Parameters of 187Re Complexes for Designing New MRI Probes: From the Gas Phase to Solution and a Model Protein Environment |
| title_sort | exploring epr parameters of 187re complexes for designing new mri probes from the gas phase to solution and a model protein environment |
| url | http://dx.doi.org/10.1155/2022/7056284 |
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