| Texto completo | |
| Autor(es): |
Almeida, Michell O.
;
Barros, Daiane A. S.
;
Araujo, Sheila C.
;
Faria, Sergio H. D. M.
;
Maltarollo, Vinicius G.
;
Honorio, Kathia M.
Número total de Autores: 6
|
| Tipo de documento: | Artigo Científico |
| Fonte: | SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY; v. 184, p. 169-176, SEP 5 2017. |
| Citações Web of Science: | 6 |
| Resumo | |
Cancer cells can expand to other parts of body through blood system and nodes from a mechanism known as metastasis. Due to the large annual growth of cancer cases, various biological targets have been studied and related to this disorder. A very interesting target related to cancer is human epidermal growth factor receptor 2 (HER2). In this study, we analyzed the main intermolecular interactions between a drug used in the cancer treatment (5fluorouracil) and HER2. Molecular modeling methods were also employed to assess the molecular structure, spectroscopic properties (FTIR and UV-Vis), NBO, QTAIM and HOMO-LUMO energies of 5-FU. From the docking simulations it was possible to analyze the interactions that occur between some residues in the binding site of HER2 and 5-FU. To validate the choice of basis set that was used in the NBO and QTAIM analyses, theoretical calculations were performed to obtain FT-IR and UV/Vis spectra, and the theoretical results are consistent with the experimental data, showing that the basis set chosen is suitable. For the maximum K from the theoretical calculation (254.89 nm) of UV/Vis, the electronic transition from HOMO to LUMO occurs at 4.89 eV. From NBO analyses, we observed interactions between Asp863 and 5-FU, i.e. the orbitals with high transfer of electrons are LP 015 (donor NBO) and BD{*} (pi) N-1-H-10 (acceptor NBO), being that the value of this interaction is 7.72 kcal/mol. Results from QTAIM indicate one main intermolecular H bond, which is necessary to stabilize the complex formed between the ligands and the biological target. Therefore, this study allowed a careful evaluation on the main structural, spectroscopic and electronic properties involved in the interaction between 5-FU and HERZ, an important biological complex related to the cancer treatment. (C) 2017 Elsevier B.V. All rights reserved. (AU) | |
| Processo FAPESP: | 14/27189-9 - Estudo teórico da interação entre ligantes bioativos e o receptor TGF-² tipo 1 (ALK-5) empregando métodos de modelagem molecular |
| Beneficiário: | Michell de Oliveira Almeida |
| Modalidade de apoio: | Bolsas no Brasil - Doutorado |