Human neuropeptide substance P self-assembles into semi-flexible nanotubes that can be manipulated for nanotechnology
Source abstract
Abstract
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.
Source: openalex_inverted_index · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Supramolecular Self-Assembly in Materials · Silk-based biomaterials and applications · Diatoms and Algae Research
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
School of Health and Biomedical Sciences
Translational Immunology and Nanotechnology (TIN) Program
RMIT University
Bundoora VIC3083
Australia
Laboratory of Food and Soft Materials
ETH-Zürich
CH-8092 Zürich
Switzerland
The Australian Synchrotron
ANSTO Research Facilities
Clayton VIC3168
Department of Chemistry and Physics
Institute for Molecular Science
La Trobe University
Bundoora VIC3086
School of Science
College of Science
Engineering and Health
Melbourne VIC3000
Funding
Royal Melbourne Institute of Technology · La Trobe University · Australian Research Council
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