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

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Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorUniversity of Gdańsk-
Autor(es): dc.creatorBertozo, Luiza de Carvalho-
Autor(es): dc.creatorKogut, Małgorzata-
Autor(es): dc.creatorMaszota-Zieleniak, Martyna-
Autor(es): dc.creatorSamsonov, Sergey A.-
Autor(es): dc.creatorXimenes, Valdecir F.-
Data de aceite: dc.date.accessioned2025-08-21T21:58:03Z-
Data de disponibilização: dc.date.available2025-08-21T21:58:03Z-
Data de envio: dc.date.issued2023-03-01-
Data de envio: dc.date.issued2023-03-01-
Data de envio: dc.date.issued2022-10-05-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.saa.2022.121374-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/240149-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/240149-
Descrição: dc.descriptionThe 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.-
Descrição: dc.descriptionDepartment of Chemistry Faculty of Sciences UNESP – São Paulo State University, São Paulo-
Descrição: dc.descriptionFaculty of Chemistry University of Gdańsk, Wita Stwosza 63-
Descrição: dc.descriptionDepartment of Chemistry Faculty of Sciences UNESP – São Paulo State University, São Paulo-
Idioma: dc.languageen-
Relação: dc.relationSpectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectAlbumin-
Palavras-chave: dc.subjectAxial chirality-
Palavras-chave: dc.subjectBiaryl compounds-
Palavras-chave: dc.subjectInduced circular dichroism-
Palavras-chave: dc.subjectMolecular dynamics-
Palavras-chave: dc.subjectQuantum mechanics-
Título: dc.titleInduced circular dichroism as a tool to monitor the displacement of ligands between albumins-
Tipo de arquivo: dc.typelivro digital-
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