Structural changes induced in bovines serum albumin by covalent attachment of chlorogenic acid

摘要

Bovine serum albumin (BSA) was modified by covalent attachment of chlorogenic acid using different concentrations at pH 9. The derivatization was accompanied by a reduction of lysine, cysteine and tryptophan residues. The isoelectric points were shifted To lower pH values and formation of high molecular weight fractions was noted. The structural changes were studied using circular Dichroism, differential scanning caloriemtry (DSC), intrinsic fluorescence, and binding of anilinonapthalensulfonic acid. The Results showed that the content of α-helix decreased with a parallel increase in unordered structures with higher degrees of deriva- Tizaiton.