%0 Journal Article %1 WOS:000378430900004 %A Mota, K B %A Neto, J X Lima %A Costa, Lima A H %A Oliveira, J I N %A Bezerra, K S %A Albuquerque, E L %A Caetano, E W S %A Freire, V N %A Fulco, U L %C PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS %D 2016 %I ELSEVIER SCIENCE BV %J COMPUTATIONAL AND THEORETICAL CHEMISTRY %K (Density (Molecular Caps) Conjugate DFT Estrogen Fractionation Function MFCC Raloxifene, Tamoxifen} Theory); biochemistry; receptor; scheme; with {Quantum %P 21-27 %R 10.1016/j.comptc.2016.05.006 %T A quantum biochemistry model of the interaction between the estrogen receptor and the two antagonists used in breast cancer treatment %V 1089 %X In this work we employed quantum biochemistry methods based on the density functional theory (DFT) model and the MFCC (Molecular Fractionation with Conjugate Caps) scheme to unveil the detailed binding energy features of the tissue-selective synthetic agents SERMs (selective estrogen receptor modulators) 4-hydroxytamoxifen (OHT) and raloxifene (RAL), widely used in the breast cancer treatment, co-crystallized with the estrogen receptor alpha (ER alpha). Our theoretical/computational results demonstrated that the total binding energies of OHT and RAL to the ERa ligand-pocket correlate with the experimental binding affinity. Besides, we found that SERMs-OHT binds stronger when compared to SERMs-RAL, confirming experimental data, whose main contributions to the total SERMs-ER alpha binding energy are due to the amino acid residues in decreasing sequence D351 > E542 > D538 > E353 > E423, an important information to understand their binding mechanisms. (C) 2016 Elsevier B.V. All rights reserved.

@article{WOS:000378430900004, abstract = {In this work we employed quantum biochemistry methods based on the density functional theory (DFT) model and the MFCC (Molecular Fractionation with Conjugate Caps) scheme to unveil the detailed binding energy features of the tissue-selective synthetic agents SERMs (selective estrogen receptor modulators) 4-hydroxytamoxifen (OHT) and raloxifene (RAL), widely used in the breast cancer treatment, co-crystallized with the estrogen receptor alpha (ER alpha). Our theoretical/computational results demonstrated that the total binding energies of OHT and RAL to the ERa ligand-pocket correlate with the experimental binding affinity. Besides, we found that SERMs-OHT binds stronger when compared to SERMs-RAL, confirming experimental data, whose main contributions to the total SERMs-ER alpha binding energy are due to the amino acid residues in decreasing sequence D351 > E542 > D538 > E353 > E423, an important information to understand their binding mechanisms. (C) 2016 Elsevier B.V. All rights reserved.}, added-at = {2022-05-23T20:00:14.000+0200}, address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS}, author = {Mota, K B and Neto, J X Lima and Costa, Lima A H and Oliveira, J I N and Bezerra, K S and Albuquerque, E L and Caetano, E W S and Freire, V N and Fulco, U L}, biburl = {https://www.bibsonomy.org/bibtex/2b457e07fbe0e9400b6b0126372e69915/ppgfis_ufc_br}, doi = {10.1016/j.comptc.2016.05.006}, interhash = {3a8f7d7855554f0afb9e36024ce16e62}, intrahash = {b457e07fbe0e9400b6b0126372e69915}, issn = {2210-271X}, journal = {COMPUTATIONAL AND THEORETICAL CHEMISTRY}, keywords = {(Density (Molecular Caps) Conjugate DFT Estrogen Fractionation Function MFCC Raloxifene, Tamoxifen} Theory); biochemistry; receptor; scheme; with {Quantum}, pages = {21-27}, publisher = {ELSEVIER SCIENCE BV}, pubstate = {published}, timestamp = {2022-05-23T20:00:14.000+0200}, title = {A quantum biochemistry model of the interaction between the estrogen receptor and the two antagonists used in breast cancer treatment}, tppubtype = {article}, volume = 1089, year = 2016 }