Developing peptide-based drugs that selectively inhibit cancer cells would establish efficient and reliable therapeutic solutions . Membranolytic ACPs (mACPs) represent one promising avenue with remarkable selectivity towards cancer cells, evading multidrug resistance. The selectivity capability of a peptide drug is traditionally defined as the ratio of cytotoxicity to its biological activity; Badisa and co-workers established the selectivity index (SI) using IC50 values against a normal healthy cell line (HCL) and a cancer cell line (CCL). A higher SI value means greater selectivity, while a value less than 2 indicates the general toxicity of a peptide. Membranolytic ACPs have demonstrated broad-spectrum inhibition of cancer cell lines and limited toxicity against normal cells. Numerous attempts for designing selective mACPs focused on studying their physicochemical properties or the characteristics of cancer cell membranes, as summarised in comprehensive reviews . Despite their sequence heterology and origin, many mACPs presented similar physicochemical properties, including 10-30 residues in length, a net charge between +2 and +9, 40-60% hydrophobic amino acids, and they predominantly fold into α-helices. These properties sometimes correlate with an increase in activity and selectivity against targeted cancer cells. These studies have also attributed the selectivity (or lack thereof) of cationic α-helical mACPs to their interactions with negatively charged components on cancer cell surfaces (e.g., phospholipids, glycoproteins, glycolipids, proteoglycans) and characteristics such as membrane potential, membrane permeability and asymmetry , cholesterol content and cell surface area.