Cephalosporin binding sites to human serum albumin and the relation with the N-B transition of this protein.

BIBIANA BEATRIZ NERLI; F. GARCÍA; C. BALLÁN; PICÓ, G.

Biochemistry and Molecular Biology International

Academic Press Australia

Año: 1995 vol. 36 p. 177 - 184

1039-9712

The binding of some cephalosporins to human serum albumin was studied using probes for the socalled I, II, bilirubin and fatty acids binding sites. The results showed that cephradine and cefsulodin bind to site II, cefaclor, cefamandole, cefsulodin, cephaloglycin and cefadroxil bind to the bilirubin binding site, while cefaclor does it to the fatty acid binding site. No binding of these cephalosporins to site I of albumin was found. The binding produced a perturbation on the N-B equilibrium of albumin, stabilizing the N conformational form, which suggests that the N form of albumin has more affinity with the cephalosporins than the B form. This finding gives support to the assumption that the binding of cephalosporins to site II, bilirubin and fatty acids binding sites affects the N-B transition of albumin.