Esterase activity and interaction of human hemoglobin with diclofenac sodium: A spectroscopic and molecular docking study.
J Mol Recognit
; 33(8): e2841, 2020 08.
Article
en En
| MEDLINE
| ID: mdl-32150309
To get an idea about the pharmacokinetics and pharmacodynamics, it is important to study the drug-protein interaction. Therefore, herein, we studied the interaction of diclofenac sodium (DIC) with human hemoglobin. The binding study of nonsteroidal antiinflammatory drug, DIC with human hemoglobin (HHB) was done by utilizing fluorescence, UV-visible, time-resolved fluorescence and far-UV circular dichroism spectroscopy (CD). Various thermodynamic parameters such as enthalpy change (ΔH), entropy change (ΔS), and Gibbs free energy change (ΔG) were also calculated. CD results showed that DIC induces secondary structure change in HHB. Fluorescence resonance energy transfer was also performed. Additionally, it was also observed that DIC inhibits the esterase-like enzymatic activity of HHB via competitive inhibition.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Hemoglobinas
/
Diclofenaco
/
Esterasas
/
Simulación del Acoplamiento Molecular
Límite:
Humans
Idioma:
En
Revista:
J Mol Recognit
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2020
Tipo del documento:
Article
País de afiliación:
India
Pais de publicación:
Reino Unido