Water, Solute, and Ion Transport in De Novo-Designed Membrane Protein Channels

Biological organisms engineer peptide sequences to fold into membrane pore proteins capable of performing a wide variety of transport functions. Synthetic de novo-designed membrane pores can mimic this approach to achieve a potentially even larger set of functions. Here we explore water, solute, and ion transport in three de novo designed β-barrel membrane channels in the 5-10 Å pore size range. We show that these proteins form passive membrane pores with high water transport efficiencies and size rejection characteristics consistent with the pore size encoded in the protein structure. Ion conductance and ion selectivity measurements also show trends consistent with the pore size, with the two larger pores showing weak cation selectivity. MD simulations of water and ion transport and solute size exclusion are consistent with the experimental trends and provide further insights into structure-function correlations in these membrane pores.

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Publication Details

Journal
ACS Nano
Published
2024-12-23
DOI
https://doi.org/10.1021/acsnano.4c11317
Citations
6
Primary Topic
Nanopore and Nanochannel Transport Studies
Type
article
Field-Weighted Citation Impact
1.11

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article

Water, Solute, and Ion Transport in De Novo-Designed Membrane Protein Channels

Jeevapani J. Hettige, Bradley Harris, Samuel Berhanu, Aleksandr Noy et al.
6 citations
ACS Nano
Nanopore and Nanochannel Transport Studies
1.11
article

Water, Solute, and Ion Transport in De Novo-Designed Membrane Protein Channels

Jeevapani J. Hettige, Bradley Harris, Samuel Berhanu, Aleksandr Noy, Marcel D. Baer, James J. De Yoreo, David A. Baker, Yu‐Hao Li, Anastassia A. Vorobieva, Stephen C. Myers, Chenyang Shi, Zhongwu Li, Sagardip Majumder, Jobaer Abdullah
article en
6 citations

Abstract

Biological organisms engineer peptide sequences to fold into membrane pore proteins capable of performing a wide variety of transport functions. Synthetic de novo-designed membrane pores can mimic this approach to achieve a potentially even larger set of functions. Here we explore water, solute, and ion transport in three de novo designed β-barrel membrane channels in the 5-10 Å pore size range. We show that these proteins form passive membrane pores with high water transport efficiencies and size rejection characteristics consistent with the pore size encoded in the protein structure. Ion conductance and ion selectivity measurements also show trends consistent with the pore size, with the two larger pores showing weak cation selectivity. MD simulations of water and ion transport and solute size exclusion are consistent with the experimental trends and provide further insights into structure-function correlations in these membrane pores.

ACS NanoVol. 19(2)
Lawrence Livermore National Laboratory (US), Howard Hughes Medical Institute (US), Vrije Universiteit Brussel (BE), Pacific Northwest National Laboratory (US), University of California, Merced (US), University of Washington (US), VIB-VUB Center for Structural Biology (BE)
Basic Energy Sciences
Clean water and sanitation
Openalex Percentile: Top 24%
Nanopore and Nanochannel Transport Studies
1.11
DOIOpen Access PDFOpenAlex
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