Formulation and Quality – Biomolecular
2019 PharmSci 360
Evaluation of tertiary structure of protein therapeutics (lysozyme and lactoferrin) and their stability into the hydrogel is really important for developing formulations that enhance product efficacy. In this study, a Raman spectroscopy technique (Renishaw plc , United Kingdom) Specifically, characterization of protein conformational stability is obtained with Raman spectroscopy. Also their optical images were taken and evaluated with camera. Proteins in sodium hyaluronate is also evaluated by differential scanning calorimetry ( Mettler-Toledo ).
As a result using Raman spectroscopy is one of best way to understanding the conformational stability of lysozyme and lactoferrin and provides unique analytical capabilities to determine secondary and tertiary structure of proteins. The results illustrates that proteins into gel, the secondary structure changes from. α -helix abundant to ß-sheet rich structure: . α -helix drops from 35 % to 20%, and ß-sheet increases from 5% to 30%.