Using Martini 2 and 3 we simulated four α-helices 16, 19, 23, and 27 residues in length, from the WALP (tryptophan-alanine-leucine) series of peptides (termed WALP16, WALP19, WALP23, and WALP27; see Table ). We chose these peptides because their TM behavior is well established, and their tilt angle as a function of their length has been documented experimentally and with atomistic simulations . This was relevant because we wanted to probe the TM stability of peptides, prompted by recent observations that supposedly transmembranar peptides might, under Martini 3, have weaker affinity for the membrane core . Peptides were simulated embedded in a DMPC membrane, as in the atomistic simulations of ref. , above the lipid's gel-to-fluid transition temperature.