| 초록 |
Although we reported that HPA3NT3, an analogue peptide derived from HP(2-20)(peptide with residues 2-20 of Helicobacter pylori Ribosomal protein L1),was a potent antimicrobial peptide, its cytotoxicity at high concentration was considered when it was applied in vivo as an antimicrobial drug. Hence, Phe (1 and 8 position) and Asn (13 position) residues of the peptide were substituted to reduce cytotoxicity by Ala and to enhance antimicrobial actitvity by Lys, respectively, and named to HPA3NT3-A2. Interestingly, HPA3NT3 peptide exerted a potent antimicrobial activity as it forms pore in cytoplasmic membrane, while HPA3NT3-A2 peptide bound to nucleic acids and inhibited protein synthesis through penetration into cytoplasm. In addition, HPA3NT3-A2D(allLys residues by D-enantiomer) was resistant to proteolytic cleavage in human serum and its antibacterial activity was enhanced. |
