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 Santos-
Data de aceite: dc.date.accessioned2025-08-21T15:29:16Z-
Data de disponibilização: dc.date.available2025-08-21T15:29:16Z-
Data de envio: dc.date.issued2019-05-03-
Data de envio: dc.date.issued2019-05-03-
Data de envio: dc.date.issued2018-
Fonte completa do material: dc.identifierhttp://www.repositorio.ufop.br/handle/123456789/11182-
Fonte completa do material: dc.identifierhttps://www.sciencedirect.com/science/article/pii/S0308814617315674-
Fonte completa do material: dc.identifierhttps://doi.org/10.1016/j.foodchem.2017.09.092-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1016451-
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.-
Formato: dc.formatapplication/pdf-
Idioma: dc.languageen-
Direitos: dc.rightsrestrito-
Palavras-chave: dc.subjectIntermolecular interaction-
Palavras-chave: dc.subjectAnalytical technique-
Palavras-chave: dc.subjectBSA conformation-
Palavras-chave: dc.subjectPhotodegradation-
Título: dc.titleThermodynamic and kinetic analyses of curcumin and bovine serum albumin binding.-
Aparece nas coleções:Repositório Institucional - UFOP

Não existem arquivos associados a este item.