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Science 30 November 1990:
Vol. 250. no. 4985, pp. 1256 - 1259
DOI: 10.1126/science.1700867
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Articles

Science, Vol 250, Issue 4985, 1256-1259
Copyright © 1990 by American Association for the Advancement of Science

articles

Kinetics of gramicidin channel formation in lipid bilayers: transmembrane monomer association

AM O'Connell, RE Koeppe 2nd, and OS Andersen

Department of Physiology and Biophysics, Cornell University Medical College, New York, NY 10021.

Conducting gramicidin channels form predominantly by the transmembrane association of monomers, one from each side of a lipid bilayer. In single-channel experiments in planar bilayers the two gramicidin analogs, [Val1]gramicidin A (gA) and [4,4,4-F3-Val1]gramicidin A (F3gA), form dimeric channels that are structurally equivalent and have characteristically different conductances. When these gramicidins were added asymmetrically, one to each side of a preformed bilayer, the predominant channel type was the hybrid channel, formed between two chemically dissimilar monomers. These channels formed by the association of monomers residing in each half of the membrane. These results also indicate that the hydrophobic gramicidins are surprisingly membrane impermeant, a conclusion that was confirmed in experiments in which gA was added asymmetrically and symmetrically to preformed bilayers.


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