Induced circular dichroism as a tool to monitor the displacement of ligands between albumins

Detalhes bibliográficos
Autor(a) principal: Bertozo, Luiza de Carvalho [UNESP]
Data de Publicação: 2022
Outros Autores: Kogut, Małgorzata, Maszota-Zieleniak, Martyna, Samsonov, Sergey A., Ximenes, Valdecir F. [UNESP]
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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spelling 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
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