Synthesis of Parallel and Antiparallel Magainin 2 Dimers and Their Interaction with Lipid and Cell Membrane

Magainin 2 (MG2) is a cationic amphiphilic peptide isolated from the skin of the African clawed frog (Xenopus laevis) and has antibacterial activity. MG2 was found to strongly interact with anionic phospholipid to form ion channels in lipid bilayers [1,2]. The synthesis and properties of parallel dimers [3,4] and antiparallel dimer of MG2 [5] have been successively reported. In this study, we synthesized two MG2 analogs, MG2-C and MG2-N, which have a linker of βAla-Cys at the C-terminus and Cys-βAla at the N-terminus, respectively. Then, we prepared a parallel MG2 dimer (MG2-CC) from MG2-C and an antiparallel MG2 dimer (MG2-CN) from MG2-C and MG2-N (Figure 1), and investigated their properties and antibacterial activity.