Investigating freezing-induced acidity changes in citrate buffers.

Citrate buffers are commonly utilized in the field of biomolecule stabilization. We investigate their applicability in the frozen state within a range of initial pHs (2.5 to 8.

Probing the interaction between niobium pentoxide nanoparticles and serum albumin proteins by Spectroscopic approaches.

Nanoparticles (NPs) can directly or indirectly enter into the body because of their small size; then they tend to alter the conformation and function of proteins upon interaction with them. Thus, it is crucial to understand the impact of NPs in a biological medium. Recently, niobium pentoxide nanoparticles (NbO NPs) are finding increasing applications in the biological system, for example, bone tissue and dental material, matrix for biosensing of proteins, .

Making good's buffers good for freezing: The acidity changes and their elimination via mixing with sodium phosphate.

Solutions of three Good's buffers (HEPES, MOPS, and MES), both pure and mixed with sodium phosphate buffers (Na-P), are investigated in terms of the freezing-induced acidity changes in their operational pH ranges. The Good's buffers have the tendency to basify upon freezing and, more intensively, at lower pHs. The acidity varies most prominently in MES, where the change may reach the value of two.