Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides.

@article{Dathe1997HydrophobicityHM,
  title={Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides.},
  author={Margitta E Dathe and Torsten Wieprecht and Heike Nikolenko and Laura M. Handel and W. Lee Maloy and David L. MacDonald and Michael Beyermann and M. Bienert},
  journal={FEBS letters},
  year={1997},
  volume={403 2},
  pages={
          208-12
        }
}
The hydrophobicity (H), hydrophobic moment (mu) and the angle subtended by the positively charged helix face (phi) of a set of model and magainin 2 amide peptides with conserved charge and helix propensity have been shown to be effective modulators of antibacterial and haemolytic activity. Except peptides of low hydrophobicity which are inactive, changing the parameters has little influence on the activity against Gram-negative bacteria, thus revealing the dominance of electrostatic… CONTINUE READING
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