The consequence of sequence alteration of an amphipathic alpha-helical antimicrobial peptide and its diastereomers.

@article{Papo2002TheCO,
  title={The consequence of sequence alteration of an amphipathic alpha-helical antimicrobial peptide and its diastereomers.},
  author={Niv Papo and Ziv Oren and Ulrike Pag and H. -G. Sahl and Yechiel Shai},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 37},
  pages={33913-21}
}
The search for antibiotics with a new mode of action led to numerous studies on antibacterial peptides. Most of the studies were carried out with l-amino acid peptides possessing amphipathic alpha-helix or beta-sheet structures, which are known to be important for biological activities. Here we compared the effect of significantly altering the sequence of an amphipathic alpha-helical peptide (15 amino acids long) and its diastereomer (composed of both l- and d-amino acids) regarding their… CONTINUE READING