Single-chain heteropolymers transport protons selectively and rapidly
- Univ. of California, Berkeley, CA (United States); Xiamen Univ. (China)
- Univ. of California, Berkeley, CA (United States)
- Univ. of California, Santa Cruz, CA (United States); Quantapore Inc., South San Francisco, CA (United States)
- Northwestern Univ., Evanston, IL (United States)
- Univ. of California, Berkeley, CA (United States); Indiana Univ., Bloomington, IN (United States)
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
- Univ. of California, Santa Cruz, CA (United States)
- Univ. of California, Berkeley, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Precise protein sequencing and folding are believed to generate the structure and chemical diversity of natural channels, both of which are essential to synthetically achieve proton transport performance comparable to that seen in natural systems. Geometrically defined channels have been fabricated using peptides, DNAs, carbon nanotubes, sequence-defined polymers and organic frameworks. However, none of these channels rivals the performance observed in their natural counterparts. Here we show that without forming an atomically structured channel, four-monomer-based random heteropolymers (RHPs) can mimic membrane proteins and exhibit selective proton transport across lipid bilayers at a rate similar to those of natural proton channels. Statistical control over the monomer distribution in an RHP leads to segmental heterogeneity in hydrophobicity, which facilitates the insertion of single RHPs into the lipid bilayers. It also results in bilayer-spanning segments containing polar monomers that promote the formation of hydrogen-bonded chains for proton transport. Our study demonstrates the importance of the adaptability that is enabled by statistical similarity among RHP chains and of the modularity provided by the chemical diversity of monomers, to achieve uniform behaviour in heterogeneous systems. Finally, our results also validate statistical randomness as an unexplored approach to realize protein-like behaviour at the single-polymer-chain level in a predictable manner.
- Research Organization:
- Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
- Sponsoring Organization:
- National Science Foundation (NSF); US Army Research Office (ARO); USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
- Grant/Contract Number:
- AC02-05CH11231; AC05-00OR22725; FG02-08ER46539
- OSTI ID:
- 1607221
- Journal Information:
- Nature (London), Journal Name: Nature (London) Journal Issue: 7789 Vol. 577; ISSN 0028-0836
- Publisher:
- Nature Publishing GroupCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Single-chain heteropolymers transport protons selectively and rapidly
|
dataset | January 2019 |
Similar Records
Sequence Design of Random Heteropolymers as Protein Mimics
Mapping Composition Evolution through Synthesis, Purification, and Depolymerization of Random Heteropolymers
Population-based heteropolymer design to mimic protein mixtures
Journal Article
·
Thu Jan 12 19:00:00 EST 2023
· Biomacromolecules
·
OSTI ID:2470769
Mapping Composition Evolution through Synthesis, Purification, and Depolymerization of Random Heteropolymers
Journal Article
·
Wed Feb 21 19:00:00 EST 2024
· Journal of the American Chemical Society
·
OSTI ID:2469689
Population-based heteropolymer design to mimic protein mixtures
Journal Article
·
Tue Mar 07 19:00:00 EST 2023
· Nature (London)
·
OSTI ID:2229313