The relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determines their cytotoxicity
AuthorRekdal, Øystein; Haug, Bengt Erik; Kalaaji, manar; Hunter, Howard N.; Lindin, Inger; Israelsson, Ingrid; Solstad, Terese; Yang, Nannan; Brandl, Martin; Mantzilas, Dimitrios; Vogel, Hans J.
Results: The cytotoxic activity of model helical amphipathic peptides was markedly influenced by the positions of tryptophan residues in the sequence.
Conclusion: Tryptophan residues located adjacent to a hydrophobic helical portion created the most potent cytotoxic peptides.
Significance: More potent anticancer helical peptides can now be designed.