Human neuropeptide substance P self-assembles into semi-flexible nanotubes that can be manipulated for nanotechnology

Substance P neuropeptide is here reported to self-assemble into well-defined semi-flexible nanotubes. Using a blend of synchrotron small angle X-ray scattering, atomic force microscopy and other biophysical techniques, the natural peptide is shown to self-assemble into monodisperse 6 nm wide nanotub...

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Bibliographic Details
Published in:Nanoscale 2020-11, Vol.12 (44), p.2268-22687
Main Authors: Dharmadana, Durga, Adamcik, Jozef, Ryan, Timothy M, Appiah Danso, Samuel, Chong, Christopher J. H, Conn, Charlotte E, Reynolds, Nicholas P, Mezzenga, Raffaele, Valéry, Céline
Format: Article
Language:English
Subjects:
Atomic force microscopy
Humans
Microscopy, Atomic Force
Morphology
Nanostructures
Nanotechnology
Nanotubes
Neuropeptides
Peptides
Small angle X ray scattering
Substance P
Synchrotrons
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Summary:Substance P neuropeptide is here reported to self-assemble into well-defined semi-flexible nanotubes. Using a blend of synchrotron small angle X-ray scattering, atomic force microscopy and other biophysical techniques, the natural peptide is shown to self-assemble into monodisperse 6 nm wide nanotubes, which can closely associate into nano-arrays with nematic properties. Using simple protocols, the nanotubes could be precipitated or mineralised while conserving their dimensions and core-shell morphology. Our discovery expands the small number of available monodisperse peptide nanotube systems for nanotechnology, beyond direct relevance to biologically functional peptide nanostructures since the substance P nanotubes are fundamentally different from typical amyloid fibrils. Substance P neuropeptide is here reported to self-assemble into well-defined semi-flexible nanotubes.
ISSN:2040-3364
2040-3372
DOI:10.1039/d0nr05622g