"Colloidal interactions, from weak to strong, are a key component of non-biological as well as biological processes (for example, protein-protein interactions, PPIs). Controlling and regulating these interactions is at the core of formulation development. In terms of medical formulations, controlling PPIs is key to preventing protein degradation and aggregation, which in turn is believed to increase bioavailability. For many decades, amino acids (AAs) have been widely used to stabilize biological formulations,"
"We do not even know if it is a specific biological effect as opposed to being a generic colloidal property. There have been many proposed mechanisms to explain these broad stabilization properties. Most of the literature points towards the effect of AAs in stabilizing the folded state5, yet there have been other hypotheses that consider them as molecular lubricants for proteins (hydrotropes)4. Other mechanisms involve AA strong effects on the water H-bonding structure3."
"In biological systems, the role of AAs in the cytosol of cells has been a topic of investigation for years. It was reported that almost all water-stressed organisms reduce the aggregation of proteins in cells by raising the concentration of AAs such as proline and glutamic acid6. For example, Escherichia coli regulates cytosolic proline concentration to inhibit the initial aggregation process of cellular retinoic acid-binding proteins7."
Amino acids (AAs) influence colloidal interactions across biological and non-biological systems, affecting protein-protein interactions and formulation stability. Controlling PPIs prevents protein degradation and aggregation and can enhance bioavailability. AAs have long been used to stabilize biological formulations, yet the precise nature of their stabilizing effect on dispersions remains unclear and may be a generic colloidal property rather than a specific biological one. Proposed mechanisms include stabilization of folded states, hydrotropic molecular lubrication, and strong modulation of water hydrogen-bonding. In cells, increased concentrations of AAs like proline and glutamic acid correlate with reduced protein aggregation under water stress. No predictive theory currently exists to determine stabilization from independent measurements.
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