Diverse Bilayer Morphologies Achieved via α-Helix-to-β-Sheet Transitions in a Short Amphiphilic Peptide
Abstract
Transmembrane proteins are functional macromolecules that direct the flow of small molecules and ions across a lipid bilayer. Here, we propose the development of helical peptide amphiphiles that will serve as both the bilayer and the functional unit of a self-assembled peptide bilayer membrane. The peptide, K3L12, was designed not only to possess dimensions similar to that of a lipid bilayer but also to yield a structurally robust, alpha-helical bilayer. The formation of alpha-helices is pH-dependent, and upon annealing the sample, a transition from alpha-helices to $$\beta$$-sheets can be controlled, as indicated by optical and vibrational spectroscopies. Imaging the materials confirms morphologies similar to that of a lipid bilayer but rich in $$\alpha$$-helices. Annealing the samples yields a shift in the morphology from bilayers to curled disks, fibers, and sheets. The structural robustness of the material can facilitate the incorporation of many functions into the bilayer assembly.
- Authors:
-
[1];
- Argonne National Lab. (ANL), Argonne, IL (United States). Center for Nanoscale Materials
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC)
- OSTI Identifier:
- 1560015
- Grant/Contract Number:
- AC02-06CH11357
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Langmuir
- Additional Journal Information:
- Journal Volume: 35; Journal Issue: 27; Journal ID: ISSN 0743-7463
- Publisher:
- American Chemical Society
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
Citation Formats
Fry, H. Christopher, Silveira, Gleiciani de Q., Cohn, Hannah M., and Lee, Byeongdu. Diverse Bilayer Morphologies Achieved via α-Helix-to-β-Sheet Transitions in a Short Amphiphilic Peptide. United States: N. p., 2019.
Web. doi:10.1021/acs.langmuir.9b00424.
Fry, H. Christopher, Silveira, Gleiciani de Q., Cohn, Hannah M., & Lee, Byeongdu. Diverse Bilayer Morphologies Achieved via α-Helix-to-β-Sheet Transitions in a Short Amphiphilic Peptide. United States. https://doi.org/10.1021/acs.langmuir.9b00424
Fry, H. Christopher, Silveira, Gleiciani de Q., Cohn, Hannah M., and Lee, Byeongdu. Wed .
"Diverse Bilayer Morphologies Achieved via α-Helix-to-β-Sheet Transitions in a Short Amphiphilic Peptide". United States. https://doi.org/10.1021/acs.langmuir.9b00424. https://www.osti.gov/servlets/purl/1560015.
@article{osti_1560015,
title = {Diverse Bilayer Morphologies Achieved via α-Helix-to-β-Sheet Transitions in a Short Amphiphilic Peptide},
author = {Fry, H. Christopher and Silveira, Gleiciani de Q. and Cohn, Hannah M. and Lee, Byeongdu},
abstractNote = {Transmembrane proteins are functional macromolecules that direct the flow of small molecules and ions across a lipid bilayer. Here, we propose the development of helical peptide amphiphiles that will serve as both the bilayer and the functional unit of a self-assembled peptide bilayer membrane. The peptide, K3L12, was designed not only to possess dimensions similar to that of a lipid bilayer but also to yield a structurally robust, alpha-helical bilayer. The formation of alpha-helices is pH-dependent, and upon annealing the sample, a transition from alpha-helices to $\beta$-sheets can be controlled, as indicated by optical and vibrational spectroscopies. Imaging the materials confirms morphologies similar to that of a lipid bilayer but rich in $\alpha$-helices. Annealing the samples yields a shift in the morphology from bilayers to curled disks, fibers, and sheets. The structural robustness of the material can facilitate the incorporation of many functions into the bilayer assembly.},
doi = {10.1021/acs.langmuir.9b00424},
journal = {Langmuir},
number = 27,
volume = 35,
place = {United States},
year = {Wed Jun 12 00:00:00 EDT 2019},
month = {Wed Jun 12 00:00:00 EDT 2019}
}
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