In the study of anti-tumor peptide activity modification, there are many physical and chemical parameters that affect the activity of peptides, including spatial conformation, hydrophilicity, hydrophobicity, charge number, etc. These indicators restrict and influence each other. We need to comprehensively analyze various anti-tumor peptides. Physicochemical properties were screened to screen out highly active polypeptides with higher structural stability. In addition, some known anti-tumor peptides have hemolytic properties while anti-tumor, which greatly limits their clinical use. On the one hand, we can make it into a sustained-release preparation for local administration, and increase the time for its direct interaction with tumor cells to achieve the purpose of attenuating toxicity; on the other hand, while retaining the active segment of the polypeptide, it also The gene structure of the polypeptide can be modified, and anti-tumor peptides with lower hemolytic properties can be obtained through fermentation and expression. These studies have important implications for the clinical application of antitumor peptides

In the study of tumor treatment, scientists have found that peptides have great development prospects as anti-tumor drugs. Peptides have unique advantages as drugs: small molecular weight, no immunogenicity, good tissue permeability; high affinity and less side effects; solid-phase chemical synthesis of peptides makes the production cost lower than other biological drugs. There are nearly 70 kinds of peptide drugs on the market all over the world, more than 270 kinds of peptides have entered clinical research, and more than 700 kinds of peptides are in the preclinical research stage, of which more than 20 kinds of anti-tumor peptides are listed.

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