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Peptide-Functionalized Rosette Nanotubes: Programmable Supramolecular Assembly and Tunable Peptide Surface
Alaaeddin Alsbaiee1,2,3, Takeshi Yamazaki3, Mounir El Bakkari2,3
1Performance Materials Division, BASF Corporation, 1609 Biddle Avenue, Wyandotte, Michigan 48192, United States.
Biomacromolecules
|February 23, 2026
Summary
Researchers developed peptide-functionalized rosette nanotubes (RNTs) for programmable nanoscale organization. These RNTs offer a versatile platform for creating advanced biointerfaces by controlling peptide display on nanotubular surfaces.
Area of Science:
- Supramolecular Chemistry
- Nanotechnology
- Materials Science
Background:
- Rosette nanotubes (RNTs) are self-assembled nanostructures.
- Previous studies explored RNTs, but peptide functionalization requires further investigation.
Purpose of the Study:
- To investigate peptide-functionalized RNTs as scaffolds for programmable surface organization.
- To understand how peptide identity affects nanotube assembly and surface structure.
Main Methods:
- Conjugation of three distinct peptides to guanine-cytosine-inspired (G∧C) motifs.
- Characterization using electron microscopy, spectroscopy, and molecular modeling.
- Demonstration of coassembly with lysine-functionalized motifs.
Main Results:
- Peptide-functionalized RNTs self-assembled robustly in aqueous media.
- Peptide identity was shown to influence nanotube assembly and surface secondary structure.
- Controllable coassembly allowed tunable peptide density and spatial distribution.
Conclusions:
- Peptide identity dictates RNT assembly and surface properties.
- RNTs serve as a versatile platform for designing nanoscale biointerfaces.
- This study provides design principles for supramolecular peptide display on nanostructures.
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