Cationic helical peptides play a crucial role in applications such as anti‐microbial and anticancer activity. The activity of these peptides directly correlates with their helicity. In this study, we have performed extensive all‐atom molecular dynamics simulations of 25 Lysine–Leucine co‐polypeptide sequences of varying charge density () and patterns. Our findings showed that, an increase in the charge density on the peptide leads to a gradual decrease in the helicity up to a critical charge density . Beyond , a complete helix to coil transition was observed. The decrease in the helicity is correlated with the increased number of water molecules in first solvation shell, solvent‐exposed surface area, and a higher value of the radius of gyration of the peptide.