Aggregation of cateslytin beta-sheets on negatively charged lipids promotes rigid membrane domains. A new mode of action for antimicrobial peptides?

@article{JeanFranois2008AggregationOC,
  title={Aggregation of cateslytin beta-sheets on negatively charged lipids promotes rigid membrane domains. A new mode of action for antimicrobial peptides?},
  author={Frantz Jean-François and Sabine Castano and Bernard Desbat and Beno{\^i}t Odaert and Michel Roux and Marie-H{\'e}l{\`e}ne Et Metz-Boutigue and Erick J. Dufourc},
  journal={Biochemistry},
  year={2008},
  volume={47 24},
  pages={6394-402}
}
Cateslytin, a positively charged (5+) arginine-rich antimicrobial peptide (bCgA, RSMRLSFRARGYGFR), was chemically synthesized and studied against membranes that mimic bacterial or mammalian systems. Circular dichroism, polarized attenuated total reflection infrared spectroscopy, (1)H high-resolution MAS NMR, and (2)H and (31)P solid state NMR were used to follow the interaction from peptide and membrane points of view. Cateslytin, which is unstructured in solution, is converted into… CONTINUE READING