Abstract
The self-assembly of peptide nanotubes formed by an L-glutamic acid-based bolaamphiphile is shown to proceed via a remarkable mechanism where the peptide conformation changes from β-sheet to unordered. The kinetics of this process are elucidated via X-ray scattering and UV circular dichroism methods. The reverse transition from "unordered" to β-sheet structures is triggered by UV radiation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Circular Dichroism
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Furans / chemistry*
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Glutamic Acid / chemistry*
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Microscopy, Electron, Transmission
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Nanotubes, Peptide / chemistry*
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Nanotubes, Peptide / ultrastructure
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Protein Structure, Secondary
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Pyridones / chemistry*
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Scattering, Small Angle
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Spectroscopy, Fourier Transform Infrared
Substances
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Furans
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Nanotubes, Peptide
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Pyridones
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bolaamphiphile
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Glutamic Acid