Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index.

@article{Chen2005RationalDO,
  title={Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index.},
  author={Yuxin Chen and Colin T. Mant and Susan W. Farmer and Robert E. Hancock and Michael L. Vasil and Robert S. Hodges},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 13},
  pages={12316-29}
}
In the present study, the 26-residue peptide sequence Ac-KWKSFLKTFKSAVKTVLHTALKAISS-amide (V681) was utilized as the framework to study the effects of peptide hydrophobicity/hydrophilicity, amphipathicity, and helicity (induced by single amino acid substitutions in the center of the polar and nonpolar faces of the amphipathic helix) on biological activities. The peptide analogs were also studied by temperature profiling in reversed-phase high performance liquid chromatography, from 5 to 80… CONTINUE READING