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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.

Graphical abstract: Self-assembly pathway of peptide nanotubes formed by a glutamatic acid-based bolaamphiphile

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