Summarizing the MD data, the peptides from different sets demonstrate distinct differences in the size and shape of their hydrophobic patterns (Figure In conclusion, irrespective of the parent peptide, the less toxic D-mutants generally exhibit smaller and more fragmented hydrophobic surface patches. Variations in side-chain packing, driven by L/D or amino acid substitutions, result in distinct populations of backbone conformations. Peptides with high hemolytic activity (e.g., p1, 5a, 8a, 13c) predominantly adopt fold2-6 states, while those with low hemolytic activity (e.g., p3, 15c, 16c) are primarily associated with fold1-4 states. Thus, there is a relationship between backbone conformation and hemolytic behaviour in the peptide sets.