Exploring EPR Parameters of Re-187 Complexes for Designing New MRI Probes: From the Gas Phase to Solution and a Model Protein Environment
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18450%2F22%3A50019711" target="_blank" >RIV/62690094:18450/22:50019711 - isvavai.cz</a>
Result on the web
<a href="https://www.hindawi.com/journals/jchem/2022/7056284/" target="_blank" >https://www.hindawi.com/journals/jchem/2022/7056284/</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1155/2022/7056284" target="_blank" >10.1155/2022/7056284</a>
Alternative languages
Result language
angličtina
Original language name
Exploring EPR Parameters of Re-187 Complexes for Designing New MRI Probes: From the Gas Phase to Solution and a Model Protein Environment
Original language 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. © 2022 Gustavo A. Andolpho et al.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10406 - Analytical chemistry
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of chemistry
ISSN
2090-9063
e-ISSN
2090-9071
Volume of the periodical
2022
Issue of the periodical within the volume
November
Country of publishing house
GB - UNITED KINGDOM
Number of pages
8
Pages from-to
"Article number: 7056284"
UT code for WoS article
000893545700001
EID of the result in the Scopus database
2-s2.0-85143366407