Design of potent, non-toxic anticancer peptides based on the structure of the antimicrobial peptide, temporin-1CEa

摘要: Recent advances in the search for novel anticancer agents have indicated that positively charged antimicrobial peptides emerged as promising offering several advantages over conventional drugs. As a naturally occurring, cationic, α-helical peptide, temproin-1CEa has been proved to exhibit potent effect and moderate hemolytic activity. In order reduce activity of temporin-1CEa improve its potency towards range human breast cancer cells, present study, six analogs were rationally designed synthesized. The amphipathicity levels structural patterns reserved, while their cationic property hydrophobicity changed. results MTT hemolysis assay analog displayed an improved showed overall optimized therapeutic index. was correlated with antitumor activities. Moreover, data suggest strategy increasing cationicity maintaining occurring amphipathic generate cytotoxicity against tumor cells but decreased non-neoplastic such erythrocytes. This work highlights potential rational design synthesis capability be used therapeutically treatment cancers.