Arginine binds with its bidentate guanidine group tightly to phosphate groups and induces membrane thinning . The side chain length of arginine enables interaction with phosphates in the distal leaflet of the membrane, especially when a pore opens, and the specific distance between the backbone and the guanidine group is a fundamental characteristic to promote cellular uptake . Lysine, though less efficient in translocation compared to Arginine [207], can "snorkel" to stabilize a pore, a property it shares with arginine . Tryptophan is well known for its membrane-insertion capabilities, which support effective peptide anchoring . These characteristics suggest that membrane-targeting mechanisms are likely predominant among ABPs. Additionally, the observation that ABPs are shorter and typically more structured compared to AMPs may suggest that extracellular matrix selects for more compact structures, while larger and more flexible conformations can get stuck in this dense web of polymers.