The Peptide Cleavage and Purification

Specific steps of the peptide cleavage process：

1) Selection of cleavage reagents

It is crucial to select a suitable cleavage reagent based on the peptide sequence and properties. Commonly used cleavage reagents include (TFA), (HCl), etc.

2) Cleavage process

        Mix the peptide with the cleavage reagent, heat it to a certain temperature, and keep it for a certain time to break the peptide chain. This step is the key to releasing the peptide synthesized on the solid phase carrier.

3) Cooling

After the cleavage is completed, cool the reaction solution to room temperature to stop the cleavage reaction.

4) Centrifugation

Centrifuge the reaction solution to remove insoluble substances, such as resins.

5) Solvent extraction

Extract the supernatant after centrifugation with an appropriate solvent to remove the cleavage reagent and other impurities.

Peptide purification:

Purification is an important step after cleavage, the purpose of which is to remove impurities and separate the target peptide.

1) Purification method selection

According to the properties of the peptide, select an appropriate purification method, such as ion exchange chromatography, gel filtration, reverse phase chromatography, etc.

 2) Purification process

       Purify the peptide solution through the purification column.

3) Elution

Elute the peptide on the purification column with an appropriate solvent.

4) Freeze drying

Freeze-dry the purified peptide solution to obtain peptide powder.

The peptide cleavage technology process is an important link in peptide production. The technology and steps involved have a key impact on ensuring the quality and efficiency of the final product. With the advancement of biotechnology and the growth of market demand, peptide cleavage technology is also constantly being optimized and innovated, providing a solid foundation for the development of the biomedical field.