Interaction of alphaS1-casein with curcumin and its biological implications.
J Agric Food Chem
; 57(21): 10386-91, 2009 Nov 11.
Article
en En
| MEDLINE
| ID: mdl-19831420
alpha(S1)-Casein is one of the major protein components of the casein fraction of milk. Curcumin (diferuloyl methane), the major curcuminoid, constituting about 2-5% of turmeric (Curcuma longa ) is the active ingredient with many physiological, biochemical, and pharmacological properties. On the basis of spectroscopic measurements, it is inferred that curcumin binds to alpha(S1)-casein at pH 7.4 and 27 degrees C with two binding sites, one with high affinity [(2.01 +/- 0.6) x 10(6) M(-1)] and the other with low affinity [(6.3 +/- 0.4) x 10(4) M(-1)]. Binding of curcumin to alpha(S1)-casein is predominantly hydrophobic in nature. The anisotropy of curcumin or conformation of alpha(S1)-casein did not change on interaction. The stability of curcumin in solution at pH 7.2 was enhanced on binding with alpha(S1)-casein. The chaperone-like activity of alpha(S1)-casein gets slightly enhanced on its binding to curcumin. The ability of curcumin to protect erythrocytes against hemolysis was not affected due to curcumin- alpha(S1)-casein interaction. The two binding sites of alpha(S1)-casein for curcumin, along with enhanced solution stability on interaction, may offer an alternative approach in physiological and nutritional applications.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Caseínas
/
Curcumina
Límite:
Animals
Idioma:
En
Revista:
J Agric Food Chem
Año:
2009
Tipo del documento:
Article
País de afiliación:
India
Pais de publicación:
Estados Unidos