Cyclotides are cyclic antimicrobial peptides (APs) that offer promising features for the development of efficient pharmaceutical therapies. Their efficacy is still hampered by lack of molecular details of their mechanism/mode of action. We have used unconstrained an all-atom molecular dynamics (MD) simulation to investigate the interactions between a representative cyclotide (kalata B1) and bilayers comprising 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol (POPG), and 1-palmitoyl-2-oleoylphosphatidylcholine (POPC) lipids. Kalata B1 is attracted to the surface of both lipid layers through close contact interactions. There is preferential binding on POPE,POPG layer as opposed to POPC mainly due to stronger electrostatic interactions. Kalata B1 in the last 60 ns of the simulation remains in close contact with the lipid headgroups of POPE using 5 amino acid residues (VAL, ASN, THR, GLU, TRP). This initial data suggest that these surface interactions promote peptide distribution similar to the carpet model mechanism of interaction.