Antimicrobial peptides may be regarded as a potential source of future antibiotics, and the modes of action have implicated the cationic and hydrophobic nature of their interaction with bacterial membranes. In the pre...Antimicrobial peptides may be regarded as a potential source of future antibiotics, and the modes of action have implicated the cationic and hydrophobic nature of their interaction with bacterial membranes. In the present study, a 16-residue peptide (LGR16) was developed with the aim of examining the feasibility of designing an antimicrobial peptide by segregating hydrophobic residues in the nonpolar side and positively charged residues in the polar side, based on the helical wheel projections. Antimicrobial activity, hemolytic activity, cytotoxicity against mammalian cells and bactericidal kinetics were investigated to fully evaluate the biological function of the peptide. The results showed that the peptide LGR16 had strong antimicrobial activity, and its MICs against Gram-negative and Gram-positive bacteria were 8 and 4 μg/mL, respectively. LGR16 also exhibited rapid bactericidal action and had totally eradicated the bacteria at 10 min. LGR16 showed only weak hemolysis against chicken red blood cells and cytotoxicity aginst Vero cells at its MICs, and the concentration that caused 50% hemolysis exceeded its MICs 8-fold. Overall, antimicrobial peptides can be designed by assembling hydrophobic residues in the hydrophobic side and basic residues in the opposite side. The peptide LGR16 may be developed as a prospective candidate for an antimicrobial drug.展开更多
文摘Antimicrobial peptides may be regarded as a potential source of future antibiotics, and the modes of action have implicated the cationic and hydrophobic nature of their interaction with bacterial membranes. In the present study, a 16-residue peptide (LGR16) was developed with the aim of examining the feasibility of designing an antimicrobial peptide by segregating hydrophobic residues in the nonpolar side and positively charged residues in the polar side, based on the helical wheel projections. Antimicrobial activity, hemolytic activity, cytotoxicity against mammalian cells and bactericidal kinetics were investigated to fully evaluate the biological function of the peptide. The results showed that the peptide LGR16 had strong antimicrobial activity, and its MICs against Gram-negative and Gram-positive bacteria were 8 and 4 μg/mL, respectively. LGR16 also exhibited rapid bactericidal action and had totally eradicated the bacteria at 10 min. LGR16 showed only weak hemolysis against chicken red blood cells and cytotoxicity aginst Vero cells at its MICs, and the concentration that caused 50% hemolysis exceeded its MICs 8-fold. Overall, antimicrobial peptides can be designed by assembling hydrophobic residues in the hydrophobic side and basic residues in the opposite side. The peptide LGR16 may be developed as a prospective candidate for an antimicrobial drug.
