Polypeptide synthesis is a process of repeated addition of amino acids, usually from the c terminal to the N terminal (amino terminal). The principle of solid phase synthesis of polypeptides is to connect the C-terminal of the first amino acid of the target peptide with the solid phase carrier through a covalent bond, and then take the N-terminal of the amino acid as the starting point for synthesis.
After removing the amino protection group and reacting with the excessive activated second amino acid, the peptide chain is extended, and the operation is repeated to achieve the ideal synthetic peptide chain length. Finally, the peptide chain is split off from the resin, separated and purified, and the target polypeptide is obtained
With the development of peptide synthesis, peptide liquid phase segmental synthesis (that is, the synthesis method of peptide fragments in solution based on their chemical specificity or chemical selectivity to spontaneously connect long peptides) plays an increasingly prominent role in the field of peptide synthesis. The utility model is characterized in that it can be used for the synthesis of long peptides with high purity and easy purification.
The peptide synthesis in liquid phase is mainly divided into natural chemical linkage and Staudenger linkage. Natural chemical connection is The basic method of peptide segmental synthesis is limited to the fact that the peptide must contain hemiphotolysine (Cys), thus limiting the application scope of natural chemical linking methods.
The extension of natural chemical bonding methods includes chemical region selective bonding, removable auxiliary group bonding, and photosensitive auxiliary group bonding. Staudenger linking method is another basic fragment linking method, which opens up a broader idea for peptide fragment linking. The orthogonal chemical linking method is an extension of the Staudenger linking method. The condensation rate between fragments is improved by simplifying the phosphine thioester auxiliary group
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