Doxorubicin hinders DNA condensation promoted by the protein bovine serum albumin (BSA).
Biopolymers
; 107(12)2017 Dec.
Article
en En
| MEDLINE
| ID: mdl-29058317
In this work, we have studied the interaction between the anticancer drug doxorubicin (doxo) and condensed DNA, using optical tweezers. To perform this task, we use the protein bovine serum albumin (BSA) in the working buffer to mimic two key conditions present in the real intracellular environment: the condensed state of the DNA and the abundant presence of charged macromolecules in the surrounding medium. In particular, we have found that, when doxo is previously intercalated in disperse DNA, the drug hinders the DNA condensation process upon the addition of BSA in the buffer. On the other hand, when bare DNA is firstly condensed by BSA, doxo is capable to intercalate and to unfold the DNA condensates at relatively high concentrations. In addition, a specific interaction between BSA and doxo was verified, which significantly changes the chemical equilibrium of the DNA-doxo interaction. Finally, the presence of BSA in the buffer stabilizes the double-helix structure of the DNA-doxo complexes, preventing partial DNA denaturation induced by the stretching forces.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
ADN
/
Albúmina Sérica Bovina
/
Doxorrubicina
/
Aductos de ADN
/
Antineoplásicos
Límite:
Animals
Idioma:
En
Revista:
Biopolymers
Año:
2017
Tipo del documento:
Article
País de afiliación:
Brasil
Pais de publicación:
Estados Unidos