The Journal of Membrane Biology

, Volume 31, Issue 1, pp 171–188

Formation of ion channels by a negatively charged analog of gramicidin a

Authors

  • H. -J. Apell
    • Department of BiologyUniversity of Konstanz
  • E. Bamberg
    • Department of BiologyUniversity of Konstanz
  • H. Alpes
    • Department of BiologyUniversity of Konstanz
  • P. Läuger
    • Department of BiologyUniversity of Konstanz
Article

DOI: 10.1007/BF01869403

Cite this article as:
Apell, H.-., Bamberg, E., Alpes, H. et al. J. Membrain Biol. (1977) 31: 171. doi:10.1007/BF01869403

Summary

O-pyromellitylgramicidin is a derivative of gramicidin in which three carboxyl groups are introduced at the terminal hydroxyl end of the peptide. Experiments with artificial lipid membranes indicate that this negatively charged analog forms ion-permeable channels in a way similar to that of gramicidin. If O-pyromellitylgramicidin is added to only one aqueous solution, the membrane conductance remains small, but increases by several orders of magnitude if the same amount is also added to the other side. In accordance with the dimer model of the channel, the membrane conductance under symmetrical conditions is proportional to the square of the aqueous concentration of O-pyromellitylgramicidin over a wide range. The ratioΜPG/ΜG of the single-channel conductance of O-pyromellitylgramicidin to that of gramicidin is close to unity at high ionic strength, but increases more than fivefold at smaller ionic strength (0.01m). This observation is explained in terms of an electrostatic effect of the fixed negative charges localized near the mouth of the channel. In a mixture of O-pyromellitylgramicidin and gramicidin, unit conductance steps of intermediate size are observed in addition to the conductance steps corresponding to the pure compounds, indicating the formation of hybrid channels. Hybrid channels with preferred orientation may be formed if small amounts of gramicidin and O-pyromellitylgramicidin are added to opposite sides of the membrane. These hybrid channels show a distinct asymmetry in the current-voltage characteristic.

Copyright information

© Springer-Verlag New York Inc 1977