RV-23, a Melittin-Related Peptide with Cell-Selective Antibacterial Activity and High Hemocompatibility
2016
Zhang, S.K., Institute of Transfusion Medicine, Beijing, China | Ma, Q., Institute of Transfusion Medicine, Beijing, China | Li, S.B., Institute of Transfusion Medicine, Beijing, China | Gao, H.W., Institute of Transfusion Medicine, Beijing, China | Tan, Y.X., Institute of Transfusion Medicine, Beijing, China | Gong, F., Institute of Transfusion Medicine, Beijing, China | Ji, S.P., Institute of Transfusion Medicine, Beijing, China
RV-23 is a melittin-related antibacterial peptide (MRP) with lower cytotoxicity than either melittin or AR-23, another MRP. The aim of this study was to explore the mechanism of RV- 23’s antibacterial selectivity and its hemocompatibility. The results showed that all the peptides exhibited lytic activity against Staphylococcus aureus and Escherichia coli, with RV-23 showing the highest potency. Moreover, RV-23 had lower cytotoxicity than melittin or AR-23 at their minimal inhibitory concentration. In addition, CD experiments showed that melittin, RV-23, and AR-23 all had a typical alpha-helical structure, and RV-23 had the lowest alpha-helix content. The structural information showed that RV-23 has the lowest hydrophobicity and highest hydrophobic moment. Because hydrophobicity and alpha-helix content are believed to correlate with hemolysis, the results indicate that the selective lytic activity against bacteria of RV-23 may be due to its low hydrophobicity and alpha-helicity, which lead to low cytotoxicity without affecting antibacterial activity. Furthermore, RV-23 did not affect the structure and function of blood components such as red blood cells, platelets, albumin, and the blood coagulation system. In conclusion, RV-23 is a cell-selective antibacterial peptide with high hemocompatibility due to its unique structure.
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