The thermal stability of bovine serum albumin (BSA) in the aqueous solutions containing the biological buffers, N-[tris(hydroxymethyl)methyl]-2-aminoethanesulfonic acid (TES), N-[tris(hydroxylmethyl)methyl]-3-aminopropanesulfonic acid (TAPS), and N-[tris(hydroxymethyl)methyl]-3-amino-2-hydroxypropanesulfonic acid (TAPSO), was studied by using dynamic light scattering (DLS) at various temperatures and concentration ranges of buffers. It is found that the increase of the buffer concentration enhanced the thermal stability of protein BSA, and the stabilization tendency follows the order of TAPSO > TES approximate to TAPS. In this study, we have also investigated the interactions of BSA with TES, TAPS, and TAPSO by using various techniques, such as UV-vis absorption, fluorescence, and molecular docking. It is revealed that the main interactions between the studied buffers and the peptide moieties of proteins are electrostatic including hydrogen bonds. The results obtained from this series of studies confirmed that the biological buffers, TES, TAPS, and TAPSO can serve as good stabilizers for the globular protein BSA, in the aqueous solutions. (C) 2013 Elsevier Ltd. All rights reserved.