Dynamics and energetics of bovine lactoferrin and phenylmethane dyes interaction followed by surface plasmon resonance

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MetadadosDescriçãoIdioma
Autor(es): dc.creatorPaula, Hauster Maximiler Campos de-
Autor(es): dc.creatorCoelho, Yara Luiza-
Autor(es): dc.creatorCastro, Alan Stampini Benhame de-
Autor(es): dc.creatorMarques, Isabela Araujo-
Autor(es): dc.creatorHudson, Eliara Acipreste-
Autor(es): dc.creatorRezende, Jaqueline de Paula-
Autor(es): dc.creatorPires, Ana Clarissa dos Santos-
Autor(es): dc.creatorSilva, Luis Henrique Mendes da-
Data de aceite: dc.date.accessioned2026-02-09T12:28:03Z-
Data de disponibilização: dc.date.available2026-02-09T12:28:03Z-
Data de envio: dc.date.issued2023-02-22-
Data de envio: dc.date.issued2023-02-22-
Data de envio: dc.date.issued2022-10-
Fonte completa do material: dc.identifierhttps://repositorio.ufla.br/handle/1/56047-
Fonte completa do material: dc.identifierhttps://www.sciencedirect.com/science/article/pii/S0927776522004775-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1161867-
Descrição: dc.descriptionAlthough toxic and dangerous, Phenylmethane (PhM) dyes have a variety of medicinal functions. To optimize the use of these dyes, it is essential to understand their interaction mechanism with proteins. Through surface plasmon resonance, we investigated the kinetics and thermodynamics of interaction between bovine lactoferrin (BLF) and PhM dyes at pH 7.4, which allowed elucidate the effect of the dyes’ functional groups on the binding process. Negative ΔG° revealed that at thermodynamic equilibrium the formed [BLF-PhM]° complex was more stable than the free BLF and PhM molecules. The increase in the number of methyl groups in the PhM structure led to an increase in the rates of association (ka) and dissociation (kd) and the binding constant (Kb). A similar effect was observed when comparing methyl violet B (MVB) and methyl violet 6 B (MV6B), in which the charged MV6B structure promoted an increase in the ka, kd, and Kb values. By contrast, an increase in the number of phenyl groups (2–3 rings) led to a decrease in the Kb values. The [BLF-PhM]° formation was entropically driven, indicating that hydrophobic interactions are critical for stabilizing these complexes These results are beneficial for understanding the molecular dynamics of protein-dye interactions.-
Idioma: dc.languageen-
Publicador: dc.publisherElsevier-
Direitos: dc.rightsrestrictAccess-
???dc.source???: dc.sourceColloids and surfaces B: Biointerfaces-
Palavras-chave: dc.subjectLactoferrin bovine-
Palavras-chave: dc.subjectPhenylmethane dyes-
Palavras-chave: dc.subjectProtein-dye interaction-
Palavras-chave: dc.subjectThermodynamics-
Palavras-chave: dc.subjectKinetics-
Palavras-chave: dc.subjectSPR-
Palavras-chave: dc.subjectSurface plasmon resonance-
Título: dc.titleDynamics and energetics of bovine lactoferrin and phenylmethane dyes interaction followed by surface plasmon resonance-
Tipo de arquivo: dc.typeArtigo-
Aparece nas coleções:Repositório Institucional da Universidade Federal de Lavras (RIUFLA)

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