Using MMS to Measure Buffer-Induced Structural Changes in an Alpha-helix Rich Enzyme


In this study, MMS was used to characterize buffer-induced structural differences of lysozyme, a well-characterized alpha-helix rich protein, in water and three common formulation buffers: Phosphate Buffer (PB), Phosphate Buffered Saline (PBS), and Tris buffer. Absorption spectra in the Amide I region were automatically collected and processed to calculate higher-order structure (HOS) percentages and the overall structural similarities between samples in all prepared conditions. The results showed the enzyme exhibited various degrees of structural change within these different buffers, and that these changes could be quantified to inform buffer selection decisions to support ideal activity.