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Acta Pharmaceutica Sinica ; (12): 366-371, 2013.
Article in Chinese | WPRIM | ID: wpr-235658


A novel peptide, named BF2-X, was designed based on the structure-activity analysis of an analogue of Buforin II, named BF2-A. The BF2-X was a hybrid peptide containing the N-terminal residues 5 to 13 of BF2-A and three repeats of the C-terminal regular alpha-helical motif RLLR, and the residues 8 valine were replaced by leucine. The results of bioinformatics analysis had showed that compared with BF2-A, the helicity, positive charge, hydrophobicity rate and C-terminal amphipathy of BF2-X had remarkably enhanced. Both peptides showed a random coil structure in an aqueous solution, while displaying a typical alpha-helical structure in 50% trifluoroethanol solution (a membrane mimic condition). BF2-X exhibited higher alpha-helical contents than BF2-A in hydrophobic environment. BF2-X displayed potent antimicrobial activities against a broad spectrum of microorganisms. And BF2-X showed stronger antimicrobial activities against bacteria tested than parent peptide BF2-A. These results suggest that the alpha-helical content was directly correlated with the enhanced antibacterial activity. Both peptides had no hemolytic action on mouse erythrocyte.

Amino Acid Sequence , Animals , Anti-Bacterial Agents , Chemistry , Pharmacology , Antimicrobial Cationic Peptides , Chemistry , Pharmacology , Bacteria , Circular Dichroism , Hemolysis , Hydrophobic and Hydrophilic Interactions , Mice , Protein Structure, Secondary , Proteins , Chemistry , Pharmacology , Structure-Activity Relationship