Core advantages of anti-cancer peptides

The cationic/amphiphilic structure endows it with high selectivity, low drug resistance, and synergistic anticancer mechanisms (enhancing chemotherapy sensitivity and reducing normal tissue toxicity). At present, a large number of therapeutic peptide drugs have entered clinical trials or been approved for market, as shown in Table 2. There are also some anti-cancer peptides in the clinical trial stage (cyclic peptide drugs targeting VEGF have entered phase III trials), which have achieved certain effects.

The application of antimicrobial peptides currently faces some challenges, such as high synthesis costs, easy degradation and polymerization by proteases, and short half-life. To address the issue of high costs, short sequences are truncated during the design phase of anti-cancer peptide sequences; To solve the hydrolysis problem of proteases, natural amino acids can be replaced with non natural amino acids, such as designing D-enantiomeric peptides β2, 2-amino acid substitution, peptide backbone cyclization, end capping such as c-amidation, carbohydrate coating, etc; Increasing the half-life can modify the anti-cancer peptide with polyethylene glycol (PEGylation) and bind it to serum albumin or antibody fragments. It can be seen that although anti-cancer peptides have great clinical application value in tumor treatment, they still need to overcome these shortcomings and challenges in order to have a place in the field of tumor drug therapy. Therefore, further identification and discovery of more anti-cancer peptide templates and anti-tumor mechanisms, as well as new methods to overcome the shortcomings of peptide drugs, are of great significance for the development of clinical anti-tumor therapeutic agents.