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  Design of peptide-membrane interactions to modulate single-file water transport through modified gramicidin channels.

Portella, G., Polupanow, T., Zocher, F., Boytsov, D. A., Pohl, P., Diederichsen, U., et al. (2012). Design of peptide-membrane interactions to modulate single-file water transport through modified gramicidin channels. Biophysical Journal, 103(8), 1698-1705. doi:10.1016/j.bpj.2012.08.059.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-15D7-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-47C8-5
Genre: Journal Article

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 Creators:
Portella, G., Author
Polupanow, T., Author
Zocher, F., Author
Boytsov, D. A., Author
Pohl, P., Author
Diederichsen, U., Author
de Groot, B. L.1, Author              
Affiliations:
1Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              

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 Abstract: Water permeability through single-filechannels is affected by intrinsic factors such as their size and polarity and by external determinants like their lipid environment in the membrane. Previous computational studies revealed that the obstruction of the channel by lipid headgroups can be long-lived, in the range of nanoseconds, and that pore-length-matching membrane mimetics could speed up water permeability. To test the hypothesis of lipid-channel interactions modulating channel permeability, we designed different gramicidin A derivatives with attached acyl chains. By combining extensive molecular-dynamics simulations and single-channel water permeation measurements, we show that by tuning lipid-channel interactions, these modifications reduce the presence of lipid headgroups in the pore, which leads to a clear and selective increase in their water permeability.

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Language(s): eng - English
 Dates: 2012-10-172012
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.bpj.2012.08.059
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Title: Biophysical Journal
Source Genre: Journal
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Pages: - Volume / Issue: 103 (8) Sequence Number: - Start / End Page: 1698 - 1705 Identifier: -