To obtain an insight into the role of hydration layers and peptide backbone in the stabilization of BSA by these buffers, we have also explored the phase transition of a thermoresponsive polymer, poly( N-isopropylacrylamide (PNIPAM)), a model compound for protein, in aqueous solutions of HEPES, EPPS, HEPES–Na, and MOPS–Na buffers at different concentrations. The stabilization tendency follows the order of MOPS–Na > HEPES–Na > HEPES ≫ EPPS. These buffers behave as a potential stabilizer for the native structure of BSA against thermal denaturation. The investigated buffers include 4-(2-hydroxyethyl)piperazine-1-ethanesulfonic acid (HEPES), 4-(2-hydroxyethyl)-1-piperazine-propanesulfonic acid (EPPS), 4-(2-hydroxyethyl)piperazine-1-ethanesulfonic acid sodium salt (HEPES–Na), and 4-morpholinepropanesulfonic acid sodium salt (MOPS–Na). In this study, we have analyzed the influence of four biological buffers on the thermal stability of bovine serum albumin (BSA) using dynamic light scattering (DLS).

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