SAAP-148 (Synthetic Antimicrobial and Anti-biofilm Peptide 148) was designed by increasing the cationicity and helicity of the random coil C-terminal region of LL-37 . In a study by Adélaïde et al. , both in vitro and in silico techniques were 2.1 Membrane-active AMPs employed to assess SAAP-148's activity against membrane models. The authors found that cholesterol and certain lipid head groups impaired SAAP-148's membrane activity, preventing it from being toxic towards red blood cells (RBCs) or other mammalian cells . However, SAAP-148 demonstrated increased interaction with bacterial membrane models, resulting in enhanced ordering of the acyl chains, likely contributing to its antimicrobial activity .