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Persistent URL http://purl.org/net/epubs/work/54980519
Record Status Checked
Record Id 54980519
Title Controlling 1D Nanostructures and Handedness by Polar Residue Chirality of Amphiphilic Peptides
Contributors
Abstract Peptide assemblies are promising nanomaterials, with their properties and technological applications being highly hinged on their supramolecular architectures. Here, how changing the chirality of the terminal charged residues of an amphiphilic hexapeptide sequence Ac-I4K2-NH2 gives rise to distinct nanostructures and supramolecular handedness is reported. Microscopic imaging and neutron scattering measurements show thin nanofibrils, thick nanofibrils, and wide nanotubes self-assembled from four stereoisomers. Spectroscopic and solid-state nuclear magnetic resonance (NMR) analyses reveal that these isomeric peptides adopt similar anti-parallel beta-sheet secondary structures. Further theoretical calculations demonstrate that the chiral alterations of the two C-terminal lysine residues cause the formation of diverse single beta-strand conformations, and the final self-assembled nanostructures and handedness are determined by the twisting direction and degree of single beta-strands. This work not only lays a useful foundation for the fabrication of diverse peptide nanostructures by manipulating the chirality of specific residues but also provides a framework for predicting the supramolecular structures and handedness of peptide assemblies from single molecule conformations.
Organisation ISIS , ISIS-LOQ , STFC
Keywords RB1720295
Funding Information NNSFC (22072181); NNSFC (22172193); NNSFC (U1832108); Postdoctoral Research Foundation of China (2021M693205)
Related Research Object(s):
Licence Information:
Language English (EN)
Type Details URI(s) Local file(s) Year
Journal Article Small 20, no. 5 (2024): 2304424. doi:10.1002/smll.202304424 2024