Ways To Improve The Stability Of Peptides

1. Site-directed mutagenesis

The stability of the polypeptide can be improved by genetically replacing the residue causing the instability of the polypeptide or introducing a residue which increases the stability of the polypeptide.

2. Chemical modification

There are many chemical modification methods for peptides, and most of them are PEG modifications. PEG is a water-soluble polymer compound that is degradable and non-toxic in the body. The combination of PEG and polypeptide can improve the solubility of the polypeptide, can adjust the biocompatibility, improve the thermal stability, resist the degradation of the protease, reduce the antigenicity, and prolong the half-life in the body. Choosing the appropriate modification method and controlling the degree of modification can improve the activity of the original organism.

3. Additives

The stability of the polypeptide can be increased by the addition of additives such as sugars, polyols, gelatin, amino acids and certain salts. Sugars and polyols force more water molecules around the protein at low concentrations, thus increasing the stability of the polypeptide. During lyophilization, the above materials may also replace water to form hydrogen bonds with the polypeptide to stabilize the native conformation of the polypeptide, and may also increase the glass transition temperature of the lyophilized product. In addition, surfactants such as SDS, Tween, and Pluronic prevent adsorption, aggregation, and precipitation of the polypeptide surface.

4. Freeze-dried

A series of chemical reactions in which peptides occur, such as deamidation, β-elimination, hydrolysis, etc., require water to participate, and water can also act as a mobile phase for other reactants. In addition, a decrease in water content can increase the denaturation temperature of the polypeptide. Thus, lyophilization increases the stability of the polypeptide.

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