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LMU researchers develop hybrid protein-foldamer nanostructures
Researchers at Ludwig-Maximilians-Universität München (LMU), led by Professor Ivan Huc, have developed an artificial protein-foldamer pair capable of creating precise hybrid nanostructures. The study, published in Nature Chemistry, addresses the difficulty of combining biological proteins with synthetic molecules with high structural precision.
By utilizing the ribosome display method, the team identified the C10 variant of a nanofitin protein scaffold. This specific protein binds with high affinity to the right-handed P-helix of a synthetic foldamer, creating a large and clearly defined contact surface. This modular building block allows for the construction of complex molecular architectures and networks that do not exist in nature.
The resulting hybrid complexes can produce nanostructures with 5nm cavities, offering new possibilities for the development of advanced artificial materials.
Entities
Ivan Huc · Ludwig-Maximilians-Universität München · Nature Chemistry
Claims
What the coverage asserts, and how many sources carry each claim.
- [○ 1 SOURCE] The study was published in the journal Nature Chemistry in August 2026. www.ad-hoc-news.de
- [● 3 SOURCES] The research team identified the C10 variant of a nanofitin protein scaffold using ribosome display. www.ad-hoc-news.de · www.bionity.com · www.chemie.de
- [○ 1 SOURCE] The developed hybrid nanostructures feature 5nm cavities. www.ad-hoc-news.de
- [● 2 SOURCES] The right-handed P-helix of the foldamer binds to the C10 protein, while no binding was found for the left-handed M-helix. www.bionity.com · www.chemie.de
- [● 3 SOURCES] Researchers led by Ivan Huc developed an artificial protein-foldamer pair. www.ad-hoc-news.de · www.bionity.com · www.chemie.de