Diverse Bilayer Morphologies Achieved via α-Helix-to-β-Sheet Transitions in a Short Amphiphilic Peptide
| Autor: | H. Christopher Fry, Hannah M. Cohn, Byeongdu Lee, Gleiciani de Q. Silveira |
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| Rok vydání: | 2019 |
| Předmět: |
Materials science
Surface Properties Lipid Bilayers Beta sheet Peptide 02 engineering and technology 010402 general chemistry 01 natural sciences Protein Structure Secondary Surface-Active Agents Protein structure Amphiphile Electrochemistry General Materials Science Particle Size Lipid bilayer Spectroscopy chemistry.chemical_classification Bilayer Temperature Surfaces and Interfaces Hydrogen-Ion Concentration 021001 nanoscience & nanotechnology Condensed Matter Physics 0104 chemical sciences Crystallography Membrane chemistry Peptides 0210 nano-technology Macromolecule |
| Zdroj: | Langmuir. 35:8961-8967 |
| ISSN: | 1520-5827 0743-7463 |
| Popis: | 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, α-helical bilayer. The formation of α-helices is pH-dependent, and upon annealing the sample, a transition from α-helices to β-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 α-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. |
| Databáze: | OpenAIRE |
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