skip to main content
Idioma:
Tipo de recurso Mostra resultados com: Mostra resultados com: Índice

Synthesis, thermodynamic properties and BSA interaction of a new Valen Shiff base derived from o-vanillin and trimethoprim

Li, Xu ; Jiang, Jian-Hong ; Xiao, Sheng-Xiong ; Gu, Hui-Wen ; Li, Chuan-Hua ; Ye, Li-Juan ; Li, Xia ; He, Du-Gui ; Yao, Fei-Hong ; Li, Qiang-Guo

Thermochimica acta, 2014-01, Vol.575, p.291-299 [Periódico revisado por pares]

Elsevier B.V

Texto completo disponível

Citações Citado por
  • Título:
    Synthesis, thermodynamic properties and BSA interaction of a new Valen Shiff base derived from o-vanillin and trimethoprim
  • Autor: Li, Xu ; Jiang, Jian-Hong ; Xiao, Sheng-Xiong ; Gu, Hui-Wen ; Li, Chuan-Hua ; Ye, Li-Juan ; Li, Xia ; He, Du-Gui ; Yao, Fei-Hong ; Li, Qiang-Guo
  • Assuntos: Bovine serum albumin ; Constants ; Fluorescence ; Formations ; Mathematical analysis ; Molecular conformation ; o-Vanillin ; Quenching ; Serum albumin ; Standard molar enthalpy of dissolution ; Standard molar enthalpy of formation ; Trimethoprim ; Valen Shiff base
  • É parte de: Thermochimica acta, 2014-01, Vol.575, p.291-299
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
  • Descrição: A new single Valen Shiff base was synthesized and characterized. The thermodynamics properties of the Shiff base were investigated by microcalorimetry. In particular, the interaction between the synthetic Shiff base and BSA at four different temperatures has been investigated using fluorescence quenching method. •A new single Valen Shiff base was synthesized and characterized.•The thermodynamics properties of the Shiff base were investigated by microcalorimetry.•The interaction between the Shiff base and BSA has been investigated using fluorescence quenching method. A new Valen Shiff base (C22H24N4O5) was synthesized using equivalent moles of o-vanillin and trimethoprim. At 298.15K, the standard molar enthalpy of formation of the new compound was estimated to be ΔfHmΘ [C22H24N4O5(s), 298.15K]=−(696.92±1.67)kJmol−1 by microcalorimetry. In particular, the interaction between the Shiff base and bovine serum albumin (BSA) has been investigated. It was proved that the fluorescence quenching of BSA by Shiff base is a result of the formation of a Shiff base-BSA complex. Quenching constants were determined using the Sterns–Volmer equation to provide a measurement of the binding site between Shiff base and BSA. The thermodynamic parameters ΔG, ΔH, and ΔS of the system at different temperatures were calculated. What is more, the distance r between donor (Trp. 213) and acceptor (Shiff base) was obtained. Finally, synchronous fluorescence spectroscopy data has suggested the association between Shiff base and BSA changed the molecular conformation of BSA.
  • Editor: Elsevier B.V
  • Idioma: Inglês;Holandês
Voltar para lista de resultados

  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

Buscando em bases de dados remotas. Favor aguardar.