Circular dichroism spectrum of (R)-(+)-3,3′-dibromo-1,1′-bi-2-naphthol in albumin: Alterations caused by complexation—Experimental and in silico investigation

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorUniversidade Estadual de Campinas (UNICAMP)-
Autor(es): dc.creatorXimenes, Valdecir Farias-
Autor(es): dc.creatorYoguim, Maurício Ikeda-
Autor(es): dc.creatorde Souza, Aguinaldo Robinson-
Autor(es): dc.creatorMorgon, Nelson Henrique-
Data de aceite: dc.date.accessioned2025-08-21T22:42:48Z-
Data de disponibilização: dc.date.available2025-08-21T22:42:48Z-
Data de envio: dc.date.issued2025-04-29-
Data de envio: dc.date.issued2024-05-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1002/chir.23675-
Fonte completa do material: dc.identifierhttps://hdl.handle.net/11449/307535-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/307535-
Descrição: dc.descriptionThis study describes the interaction of human serum albumin (HSA) with the binol derivative (R)-(+)-3,3′-dibromo-1,1′-bi-2-naphthol (R-BrB), which has its optical activity based on the prohibitive energetic barrier for conversion into the enantiomer (S)-(+)-3,3′-dibromo-1,1′-bi-2-naphthol (S-BrB). The objective was to assess the ability of HSA to differentiate axial enantiomers based on their binding efficiency and their impact on the CD spectra. We discovered that both enantiomers were effective ligands, and the CD signal disappeared when equimolar amounts of R-BrB and S-BrB were simultaneously added, indicating no preference for either enantiomer. The complexation resulted in a significant signal increase at 250 nm and a bathochromic effect at 370 nm. Molecular docking simulations were performed, and the lower energy pose of R-BrB was selected for DFT calculations. The theoretical CD spectra of free and complexed R-BrB were obtained and showed alterations corroborating the experimental results. By comparing the difference spectrum (HSA:R-BrB minus HSA) with the spectrum of free RBrB in water or ethyl alcohol, we concluded that the CD signal intensification was due to the increased solubilization of R-BrB upon binding to HSA.-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionDepartment Chemistry Faculty of Science São Paulo State University (UNESP), SP-
Descrição: dc.descriptionDepartment of Physical Chemistry Institute of Chemistry Campinas State University (UNICAMP), SP-
Descrição: dc.descriptionDepartment Chemistry Faculty of Science São Paulo State University (UNESP), SP-
Descrição: dc.descriptionCNPq: #302121/2022-6-
Descrição: dc.descriptionCNPq: #310.85/2021-3-
Idioma: dc.languageen-
Relação: dc.relationChirality-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectalbumin-
Palavras-chave: dc.subjectbinols-
Palavras-chave: dc.subjectDFT-
Palavras-chave: dc.subjectibuprofen-
Palavras-chave: dc.subjectmolecular docking-
Palavras-chave: dc.subjectwarfarin-
Título: dc.titleCircular dichroism spectrum of (R)-(+)-3,3′-dibromo-1,1′-bi-2-naphthol in albumin: Alterations caused by complexation—Experimental and in silico investigation-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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