Binary 1525

The LPcin‐YK3 (purity >95%) was finally purified by reverse‐phase high‐pressure liquid chromatography (RP‐HPLC, Waters Binary 1525, USA). The correct molecular mass of the purified LPcin‐YK3 peptide was confirmed by Ultraflex III matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry (MALDI‐TOF MS) equipment (Bruker Daltonics) (Figure 2). The 10 mg/mL of α‐cyano‐4‐hydroxycinnamic acid (CHCA, Sigma, USA) matrix was used and dissolved in 30% acetonitrile and 0.1% trifluoroacetic acid (TFA). The LPcin‐YK3 peptide was dissolved in the matrix solution, and this was loaded on the plate using the dried droplet method. The mass spectrum of LPcin‐YK3 peptide was acquired after averaging 1000 laser shots in positive ion reflector mode with the mass range of 100–6000 dalton (Da). A helical wheel projection of LPcin‐YK3 demonstrated spatial segregation of its hydrophobic and charged residues (Figure 3), indicating the amphipathic nature of the LPcin‐YK3 α‐helix. The sequence of the 15 amino acid peptide LPcin‐YK3 (NKVKEWIKYLKSLFS) contains a number of basic lysine (K) residues. Magainin²² and many other AMPs also form amphipathic α‐helices under conditions similar to those used in our experiments.