Thermodynamic and kinetic analyses of curcumin and bovine serum albumin binding

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.creatorHudson, Eliara Acipreste-
Autor(es): dc.creatorPaula, Hauster Maximiler Campos de-
Autor(es): dc.creatorFerreira, Guilherme Max Dias-
Autor(es): dc.creatorFerreira, Gabriel Max Dias-
Autor(es): dc.creatorHespanhol, Maria do Carmo-
Autor(es): dc.creatorSilva, Luis Henrique Mendes da-
Autor(es): dc.creatorPires, Ana Clarissa dos S.-
Data de aceite: dc.date.accessioned2026-02-09T12:01:24Z-
Data de disponibilização: dc.date.available2026-02-09T12:01:24Z-
Data de envio: dc.date.issued2019-04-26-
Data de envio: dc.date.issued2019-04-26-
Data de envio: dc.date.issued2018-03-
Fonte completa do material: dc.identifierhttps://repositorio.ufla.br/handle/1/33889-
Fonte completa do material: dc.identifierhttps://www.sciencedirect.com/science/article/pii/S0308814617315674?via%3Dihub-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1152639-
Descrição: dc.descriptionBovine serum albumin (BSA)/curcumin binding and dye photodegradation stability were evaluated. BSA/curcumin complex showed 1:1 stoichiometry, but the thermodynamic binding parameters depended on the technique used and BSA conformation. The binding constant was of the order of 105 L·mol−1 by fluorescence and microcalorimetric, and 103 and 104 L·mol−1 by surface plasmon resonance (steady-state equilibrium and kinetic experiments, respectively). For native BSA/curcumin, fluorescence indicated an enthalpic and entropic driven process based on the standard enthalpy change (ΔH○F = −8.67 kJ·mol−1), while microcalorimetry showed an entropic driven binding process (ΔH○cal = 29.11 kJ·mol−1). For the unfolded BSA/curcumin complex, it was found thatp ΔH○F = −16.12 kJ·mol−1 and ΔH○cal = −42.63 kJ·mol−1. BSA (mainly native) increased the curcumin photodegradation stability. This work proved the importance of using different techniques to characterize the protein-ligand binding.-
Idioma: dc.languageen-
Publicador: dc.publisherElsevier-
Direitos: dc.rightsrestrictAccess-
???dc.source???: dc.sourceFood Chemistry-
Palavras-chave: dc.subjectCurcumin-
Palavras-chave: dc.subjectIntermolecular interaction-
Palavras-chave: dc.subjectAnalytical technique-
Palavras-chave: dc.subjectBovine serum albumin (BSA)-
Palavras-chave: dc.subjectPhotodegradation-
Título: dc.titleThermodynamic and kinetic analyses of curcumin and bovine serum albumin binding-
Tipo de arquivo: dc.typeArtigo-
Aparece nas coleções:Repositório Institucional da Universidade Federal de Lavras (RIUFLA)

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