Damage of proteins at the air/water interface: Surface tension characterizes globulin interface stability.

In the present study, we aimed to see what circumstances may cause protein damage at air/water interface and reveal the correlation between the surface properties of protein solution and the interface stability. The surface hydrophobicity and β-sheet of protein were determined by exogenous fluorescent probes, and the changes in the spatial structure of proteins were characterized by steady-state fluorescence spectroscopy. The surface tension was determined by the plate method, and such value was used to establish the correlation with the hydrophobicity and structure of the protein.

Protein Aggregation and Performance Optimization Based on Microconformational Changes of Aromatic Hydrophobic Regions.

Protein aggregation is a key concern in biopharmaceutical development and manufacturing. There is growing interest in understanding how the changes in protein microconformation affect the aggregation behavior. This study selected several representative proteins and first manipulated microconformational changes of the aromatic hydrophobic regions of proteins, especially tryptophan residues, by using amine or guanidine additives.