Peptide synthesis

r, r: Polypeptide synthesis is a
solid-phase synthesis r, r: The sequence is generally synthesized from the end (
carboxyl end r, r:) to the end (amino end). In the past, peptide synthesis was performed in solution, which was called liquid phase synthesis. Since the successful development of the solid-phase peptide synthesis method in 2008, through continuous improvement and perfection, today the solid-phase method has become a commonly used technology in peptide and
protein synthesisr,r:, showing the classic liquid The incomparable advantages of the phase synthesis method greatly reduce the difficulty of product purification in each step. Peptide synthesis is generally divided into two types: solid phase synthesis and liquid phase peptide synthesis.
< r : : br brbrr'r ' br(:b.brrr_.): > : : : Peptide synthesis technology
Editor< < r rbrrr: , >In 2010, a solid-phase peptide synthesis method was developed ( ), due to its convenient and rapid synthesis, has become the preferred method for peptide synthesis. It has also brought a revolution in peptide organic synthesis and has become an independent discipline. Solid-phase organic synthesis. The invention of solid-phase synthesis also promoted the development of peptide synthesis. Automation of synthesis. The world's first true peptide synthesizer appeared in the early 1990s.
< r rbrrr : , >: >Liquid phase synthesis
< r rbrrr : , >Synthesis is performed step by step based on the repeated addition of a single protected amino acid to the growing amino component, usually starting from the synthetic chain Starting with the terminal amino acid, the subsequent attachment of individual amino acids is achieved by using, mixed carbon anhydride, or anhydride methods. Methods include linking and protecting amino acids as linkers. Importantly, this linking reagent promotes the shrinkage between the carbon group of the protected amino acid and the free amino group of the protected amino acid to form a peptide chain, and at the same time, it produces?r by-product. However, this method suffers from side reactions that lead to racemization, or the formation of () and r in the presence of strong bases. Fortunately, these side effects can be minimized, but not completely eliminated. The method is to add a linking catalyst such as or B. In addition, this method can also be used to synthesize active ester derivatives of protected amino acids. The active esters produced in turn will spontaneously react with any other protected amino acids or peptides to form new peptides