Charge Distribution Fine-Tunes the Translocation of α-Helical Amphipathic Peptides across Membranes.

@article{Ablan2016ChargeDF,
  title={Charge Distribution Fine-Tunes the Translocation of α-Helical Amphipathic Peptides across Membranes.},
  author={Francis Dean O. Ablan and B. Logan Spaller and Kaitlyn I Abdo and Paulo F. de Almeida},
  journal={Biophysical journal},
  year={2016},
  volume={111 8},
  pages={
          1738-1749
        }
}
Hundreds of cationic antimicrobial and cell-penetrating peptides (CPPs) form amphipathic α-helices when bound to lipid membranes. Here, we test two hypotheses for the differences in the ability of these peptides to translocate across membranes. The first, which we now call the hydrophobicity hypothesis, is that peptide translocation is determined by the Gibbs energy of insertion into the bilayer from the membrane interface. The second, which we call the charge-distribution hypothesis, is that… CONTINUE READING
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