β-lactoglobulin conformation influences its interaction with caffeine

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.creatorRosa, Lívia Neves Santa-
Autor(es): dc.creatorRezende, Jaqueline de Paula-
Autor(es): dc.creatorCoelho, Yara Luiza-
Autor(es): dc.creatorMendes, Tiago Antônio Oliveira-
Autor(es): dc.creatorSilva, Luis Henrique Mendes da-
Autor(es): dc.creatorPires, Ana Clarissa dos Santos-
Data de aceite: dc.date.accessioned2026-02-09T11:09:12Z-
Data de disponibilização: dc.date.available2026-02-09T11:09:12Z-
Data de envio: dc.date.issued2022-08-01-
Data de envio: dc.date.issued2022-08-01-
Fonte completa do material: dc.identifierhttps://repositorio.ufla.br/handle/1/50785-
Fonte completa do material: dc.identifierhttps://doi.org/10.1016/j.fbio.2021.101418-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1134887-
Descrição: dc.descriptionCaffeine is a molecule with bioactive properties related to increased mental performance. Its use in food products is limited by its bitterness and self-association behavior. The complex formed by β-lactoglobulin and caffeine was characterized by fluorescence spectroscopy, isothermal titration calorimetry, and molecular docking. Fluorescence spectroscopy revealed that β-lactoglobulin interacted with caffeine to form a 1:1 stoichiometric complex. Isothermal titration calorimetry characterization of β-lactoglobulin-caffeine binding revealed a different stoichiometry (1:3). Molecular docking analysis confirmed the information obtained by the two thermodynamic evaluation techniques, showing that the best interaction occurred in the hydrophobic cavity of β-lactoglobulin. The effect of protein conformation was also evaluated by fluorescence spectroscopy. The complex stoichiometry and binding constants were from the same order as those obtained for native β-lactoglobulin. However, in contrast to the complex formation with native protein, the flexibility increase observed in the thermal unfolded protein promoted a great temperature effect on the standard enthalpy and entropy changes of interaction, indicating the presence of a balance between hydrophobic and hydrophilic forces.-
Idioma: dc.languageen-
Publicador: dc.publisherElsevier-
Direitos: dc.rightsrestrictAccess-
???dc.source???: dc.sourceFood Bioscience-
Palavras-chave: dc.subjectBioactive compounds-
Palavras-chave: dc.subjectProtein thermodynamic binding-
Palavras-chave: dc.subjectIsothermal titration calorimetry-
Palavras-chave: dc.subjectMolecular docking-
Palavras-chave: dc.subjectCompostos bioativos-
Palavras-chave: dc.subjectLigação termodinâmica de proteínas-
Palavras-chave: dc.subjectCalorimetria de titulação isotérmica-
Título: dc.titleβ-lactoglobulin conformation influences its interaction with caffeine-
Tipo de arquivo: dc.typeArtigo-
Aparece nas coleções:Repositório Institucional da Universidade Federal de Lavras (RIUFLA)

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