Induced circular dichroism as a tool to monitor the displacement of ligands between albumins
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.saa.2022.121374 http://hdl.handle.net/11449/240149 |
Resumo: | The induction of chirality in a ligand can be a powerful analytical tool for studying protein–ligand interactions. Here, we advanced by applying the technique to monitor the inversion of the induced circular dichroism (ICD) spectrum when ligands move between human and bovine serum albumin proteins (HSA and BSA). ICD experiments were performed using dimers of methyl vanillate (DVT) and vanillin (DVN). The sign and spectra shape were dependent on the albumin type. DVN presented a positive maximum in 312 nm when complexed with HSA and a negative one in BSA. It was possible to induce and follow the time-dependent displacement of the ligand from BSA (2.2 × 106 M−1) to HSA (6.6 × 105 M−1) via ICD inversion. The Molecular Mechanics Generalized Born Surface Area approach was used to calculate the binding free energy of the conformers, and a dissociation pathway for each system was proposed using Umbrella Sampling calculations. Four energy minima dihedral angle conformers were identified, and the corresponding CD spectra were calculated using the quantum chemistry approach. Then, weighted spectra for the conformationally accessible conformers were obtained based on each conformer's Boltzmann probability distribution. In conclusion, the methodology described in the manuscript might be helpful in monitoring the movement of ligands between proteins that they bind. |
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Repositório Institucional da UNESP |
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Induced circular dichroism as a tool to monitor the displacement of ligands between albuminsAlbuminAxial chiralityBiaryl compoundsInduced circular dichroismMolecular dynamicsQuantum mechanicsThe induction of chirality in a ligand can be a powerful analytical tool for studying protein–ligand interactions. Here, we advanced by applying the technique to monitor the inversion of the induced circular dichroism (ICD) spectrum when ligands move between human and bovine serum albumin proteins (HSA and BSA). ICD experiments were performed using dimers of methyl vanillate (DVT) and vanillin (DVN). The sign and spectra shape were dependent on the albumin type. DVN presented a positive maximum in 312 nm when complexed with HSA and a negative one in BSA. It was possible to induce and follow the time-dependent displacement of the ligand from BSA (2.2 × 106 M−1) to HSA (6.6 × 105 M−1) via ICD inversion. The Molecular Mechanics Generalized Born Surface Area approach was used to calculate the binding free energy of the conformers, and a dissociation pathway for each system was proposed using Umbrella Sampling calculations. Four energy minima dihedral angle conformers were identified, and the corresponding CD spectra were calculated using the quantum chemistry approach. Then, weighted spectra for the conformationally accessible conformers were obtained based on each conformer's Boltzmann probability distribution. In conclusion, the methodology described in the manuscript might be helpful in monitoring the movement of ligands between proteins that they bind.Department of Chemistry Faculty of Sciences UNESP – São Paulo State University, São PauloFaculty of Chemistry University of Gdańsk, Wita Stwosza 63Department of Chemistry Faculty of Sciences UNESP – São Paulo State University, São PauloUniversidade Estadual Paulista (UNESP)University of GdańskBertozo, Luiza de Carvalho [UNESP]Kogut, MałgorzataMaszota-Zieleniak, MartynaSamsonov, Sergey A.Ximenes, Valdecir F. [UNESP]2023-03-01T20:03:38Z2023-03-01T20:03:38Z2022-10-05info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.saa.2022.121374Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, v. 278.1386-1425http://hdl.handle.net/11449/24014910.1016/j.saa.2022.1213742-s2.0-85130874763Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengSpectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopyinfo:eu-repo/semantics/openAccess2023-03-01T20:03:38Zoai:repositorio.unesp.br:11449/240149Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T22:14:39.709827Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Induced circular dichroism as a tool to monitor the displacement of ligands between albumins |
title |
Induced circular dichroism as a tool to monitor the displacement of ligands between albumins |
spellingShingle |
Induced circular dichroism as a tool to monitor the displacement of ligands between albumins Bertozo, Luiza de Carvalho [UNESP] Albumin Axial chirality Biaryl compounds Induced circular dichroism Molecular dynamics Quantum mechanics |
title_short |
Induced circular dichroism as a tool to monitor the displacement of ligands between albumins |
title_full |
Induced circular dichroism as a tool to monitor the displacement of ligands between albumins |
title_fullStr |
Induced circular dichroism as a tool to monitor the displacement of ligands between albumins |
title_full_unstemmed |
Induced circular dichroism as a tool to monitor the displacement of ligands between albumins |
title_sort |
Induced circular dichroism as a tool to monitor the displacement of ligands between albumins |
author |
Bertozo, Luiza de Carvalho [UNESP] |
author_facet |
Bertozo, Luiza de Carvalho [UNESP] Kogut, Małgorzata Maszota-Zieleniak, Martyna Samsonov, Sergey A. Ximenes, Valdecir F. [UNESP] |
author_role |
author |
author2 |
Kogut, Małgorzata Maszota-Zieleniak, Martyna Samsonov, Sergey A. Ximenes, Valdecir F. [UNESP] |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (UNESP) University of Gdańsk |
dc.contributor.author.fl_str_mv |
Bertozo, Luiza de Carvalho [UNESP] Kogut, Małgorzata Maszota-Zieleniak, Martyna Samsonov, Sergey A. Ximenes, Valdecir F. [UNESP] |
dc.subject.por.fl_str_mv |
Albumin Axial chirality Biaryl compounds Induced circular dichroism Molecular dynamics Quantum mechanics |
topic |
Albumin Axial chirality Biaryl compounds Induced circular dichroism Molecular dynamics Quantum mechanics |
description |
The induction of chirality in a ligand can be a powerful analytical tool for studying protein–ligand interactions. Here, we advanced by applying the technique to monitor the inversion of the induced circular dichroism (ICD) spectrum when ligands move between human and bovine serum albumin proteins (HSA and BSA). ICD experiments were performed using dimers of methyl vanillate (DVT) and vanillin (DVN). The sign and spectra shape were dependent on the albumin type. DVN presented a positive maximum in 312 nm when complexed with HSA and a negative one in BSA. It was possible to induce and follow the time-dependent displacement of the ligand from BSA (2.2 × 106 M−1) to HSA (6.6 × 105 M−1) via ICD inversion. The Molecular Mechanics Generalized Born Surface Area approach was used to calculate the binding free energy of the conformers, and a dissociation pathway for each system was proposed using Umbrella Sampling calculations. Four energy minima dihedral angle conformers were identified, and the corresponding CD spectra were calculated using the quantum chemistry approach. Then, weighted spectra for the conformationally accessible conformers were obtained based on each conformer's Boltzmann probability distribution. In conclusion, the methodology described in the manuscript might be helpful in monitoring the movement of ligands between proteins that they bind. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-10-05 2023-03-01T20:03:38Z 2023-03-01T20:03:38Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.saa.2022.121374 Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, v. 278. 1386-1425 http://hdl.handle.net/11449/240149 10.1016/j.saa.2022.121374 2-s2.0-85130874763 |
url |
http://dx.doi.org/10.1016/j.saa.2022.121374 http://hdl.handle.net/11449/240149 |
identifier_str_mv |
Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, v. 278. 1386-1425 10.1016/j.saa.2022.121374 2-s2.0-85130874763 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808129407610519552 |