Basic characteristics of anticancer peptides

1.1 Currently discovered anti-cancer peptides can be divided into two categories:

Selective killing type (such as Cecropins and Magainins): targets bacteria and cancer cells, is non-toxic to normal cells, and has great potential for application;

Broad spectrum killing type (such as insect defense factor Defensins): It is destructive to bacteria, cancer cells, and normal cells.

1.2 Core structural features of anticancer peptides:

Cationic: Contains positively charged amino acids such as arginine, lysine, histidine, etc., with a net surface charge of+2~+9;

Amphiphilicity: The alpha helix or beta fold structure gives it both hydrophilic and hydrophobic surfaces (such as the hydrophobic region binding to membrane lipids, and the hydrophilic region targeting cancer cell membrane anionic components through electrostatic means)

Length diversity: typically composed of 5-40 amino acids.

Functional basis: Cationic enhancement of cancer cell membrane targeting, amphiphilic mediation of membrane disruption or intracellular signal regulation.