Simultaneous binding characterization of different chromium speciation to serum albumin.
Biometals
; 37(1): 101-113, 2024 Feb.
Article
en En
| MEDLINE
| ID: mdl-37610601
The binding process between three species of chromium and serum albumin (SA) was investigated, as well as the interaction between K2Cr2O7 and bovine serum albumin (BSA) under coexistence of different chromium forms. CrCl3, K2Cr2O7 and Crpic bound to SA spontaneously through Van der Waals force, and their binding constants were 103-104 M-1 at 298 K, respectively. K2Cr2O7 and Crpic both had strong binding affinity for BSA, and significantly affected the secondary structure of BSA and the microenvironment surrounding amino acid residues. Chromium exhibited a greater fluorescence quenching constant towards HSA than toward BSA, and K2Cr2O7 induced greater conformational changes in human serum albumin (HSA) than in BSA. A weak binding of CrCl3 to BSA had no significant effect on the binding affinity of K2Cr2O7 to BSA. K2Cr2O7 and BSA have a greater binding affinity when coexisting with Crpic, and K2Cr2O7 induces a greater conformational change in BSA.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Albúmina Sérica
/
Cromo
Límite:
Humans
Idioma:
En
Revista:
Biometals
Asunto de la revista:
BIOQUIMICA
Año:
2024
Tipo del documento:
Article
Pais de publicación:
Países Bajos