Human Serum Albumin Fibril Formation in the Presence of Ligands with Different Affinity

The effect of binding of several organic ligands with different affinities on the kinetics of fibril formation of human serum albumin under denaturing conditions is studied. The values of the fraction of the denatured form of albumin in the presence of a ligand at the incubation temperature, determined from differential scanning calorimetry data, correlate with the initial rate of fibril formation and fibril yield after the end of the process. It has been shown that stabilization of the native protein structure with strongly binding ligands is a general method of inhibiting fibril formation.