Activated Complex Approach to Describe Bovine Serum Albumin-Azure A and Bovine Serum Albumin-Azure B Intermolecular Interactions

AUTOR(ES)

Paula, Hauster M. C. de; Coelho, Yara L.; Castro, Alan S. B. de; Rezende, Jaqueline P.; Pires, Ana C. S.; Silva, Luis H. M. da

FONTE

J. Braz. Chem. Soc.

DATA DE PUBLICAÇÃO

2020-12

RESUMO

Azure A (AZA) and azure B (AZB) phenothiazine dyes are used for clinical and medical purposes, and their functions can be altered via interactions with proteins. However, no kinetics information on the interactions between phenothiazine dyes and bovine serum albumin (BSA) is available. Surface plasmon resonance was used to determine the energetic and dynamic of the BSA-AZA and BSA-AZB complexes formation at pH 7.4. At temperature ≤ 16 °C, the formation of activated (DH‡a,12°C,AZA= -310.57 kJ mol-1 and DH‡a,12 °C,AZB= -256.37 kJ mol-1) and thermodynamically stable (DH°12°C,AZA= -314.56 kJ mol-1 and DH°12°C,AZB= -265.73 kJ mol-1) complexes was driven by enthalpy, while at temperature ≥ 20 °C, by entropy, (TDS‡a,28°C,AZA= 207.49 and TDS‡a,28°C,AZB= 190.69; TDS°28°C,AZA= 277.50 and TDS°28°C,AZB= 257.26 kJ mol-1). Hydrophobic interactions were fundamental to the complex stability and the increase in number of -CH3 groups in the dyes do not affect kinetic and thermodynamic parameters. Our results could help optimize the medical and pharmaceutical applications of phenothiazine dyes.

Documentos Relacionados

• Interactions of myristic acid with bovine serum albumin: a 13C NMR study.
• Pyrogenicity and Immunogenicity of Lipid A Complexed with Bovine Serum Albumin or Human Serum Albumin
• Brdicka currents observed with bovine serum albumin and completely reduced bovine serum albumin in the presence of urea.
• Binding of Candida albicans to Immobilized Amino Acids and Bovine Serum Albumin
• CHARACTERIZATION OF INTERACTION BETWEEN BUDDLEOSIDE AND BOVINE SERUM ALBUMIN