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metadata.artigo.dc.title: Kinetics and thermodynamics of bovine serum albumin interactions with Congo red dye
metadata.artigo.dc.creator: Paula, Hauster Maximiler Campos de
Coelho, Yara Luiza
Agudelo, Alvaro Javier Patiño
Rezende, Jaqueline de Paula
Ferreira, Gabriel Max Dias
Ferreira, Guilherme Max Dias
Pires, Ana Clarissa dos Santos
Silva, Luis Henrique Mendes da
metadata.artigo.dc.subject: Surface plasmon resonance
Rate constant
Binding constant
metadata.artigo.dc.publisher: Elsevier Nov-2017
metadata.artigo.dc.identifier.citation: PAULA, 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.
metadata.artigo.dc.description.abstract: To 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.
metadata.artigo.dc.language: en_US
Appears in Collections:DQI - Artigos publicados em periódicos

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