Use este identificador para citar ou linkar para este item: http://repositorio.ufla.br/jspui/handle/1/31482
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dc.creatorPaula, Hauster Maximiler Campos de-
dc.creatorCoelho, Yara Luiza-
dc.creatorAgudelo, Alvaro Javier Patiño-
dc.creatorRezende, Jaqueline de Paula-
dc.creatorFerreira, Gabriel Max Dias-
dc.creatorFerreira, Guilherme Max Dias-
dc.creatorPires, Ana Clarissa dos Santos-
dc.creatorSilva, Luis Henrique Mendes da-
dc.date.accessioned2018-10-27T14:03:08Z-
dc.date.available2018-10-27T14:03:08Z-
dc.date.issued2017-11-
dc.identifier.citationPAULA, H. M. C. de et al. Kinetics and thermodynamics of bovine serum albumin interactions with Congo red dye. Colloids and Surfaces B: Biointerfaces, [S.l.], v. 159, p. 737-742, Nov. 2017.pt_BR
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S0927776517305519pt_BR
dc.identifier.urihttp://repositorio.ufla.br/jspui/handle/1/31482-
dc.description.abstractTo optimize the therapeutic applications of Congo red (CR), a potential inhibitor of protein aggregation, the kinetics and thermodynamics of the interactions between CR and a model protein need to be understood. We used surface plasmon resonance (SPR) and fluorescence techniques to determine the dynamics and thermodynamic parameters for the formation of complexes between CR and bovine serum albumin (BSA). CR interacts with BSA through a transition complex; the activation energy for association (Eact(a)) was determined to be 35.88 kJ mol−1, while the activation enthalpy (ΔH‡), entropy (ΔS‡), and Gibbs free energy (ΔG‡) are 33.41 kJ mol−1, 0.18 J mol−1 K−1, and 33.35 kJ mol−1, respectively. When this intermediate transforms into the final CR-BSA complex, the entropy of the system increases and part of the absorbed energy is released; this process is associated with a reverse activation energy (Eact(d)) of 20.17 kJ mol−1, and values of ΔH‡, ΔS‡, and ΔG‡ of 17.69 kJ mol−1, −162.86 J mol−1 K−1, and 66.25 kJ mol−1, respectively. A comparison of the SPR and fluorescence results suggests that there is more than one site where BSA interacts with CR.pt_BR
dc.languageen_USpt_BR
dc.publisherElsevierpt_BR
dc.rightsrestrictAccesspt_BR
dc.sourceColloids and Surfaces B: Biointerfacespt_BR
dc.subjectSurface plasmon resonancept_BR
dc.subjectFluorescencept_BR
dc.subjectRate constantpt_BR
dc.subjectBinding constantpt_BR
dc.titleKinetics and thermodynamics of bovine serum albumin interactions with Congo red dyept_BR
dc.typeArtigopt_BR
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