Clavanin permeabilizes target membranes via two distinctly different pH-dependent mechanisms.

@article{Kan2002ClavaninPT,
  title={Clavanin permeabilizes target membranes via two distinctly different pH-dependent mechanisms.},
  author={Ellen J M van Kan and Rudy A. Demel and Eefjan Breukink and A van der Bent and Ben de Kruijff},
  journal={Biochemistry},
  year={2002},
  volume={41 24},
  pages={7529-39}
}
The pH dependence of the antimicrobial and membrane activity of clavanin A, a peptide antibiotic that is rich in histidines and glycines, was analyzed in growth and membrane leakage experiments. Clavanin A more effectively inhibited the growth of the test organism Lactobacillus sake when the pH of the medium was lowered. Whereas the wild-type peptide efficiently released fluorophores from unilamellar vesicles at neutral pH according to a nonspecific permeabilization mechanism, it did not… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 20 extracted citations

Similar Papers

Loading similar papers…