4.8 Article

Reassembly of Peptide Nanofibrils on Live Cell Surfaces Promotes Cell-Cell Interactions

Journal

NANO LETTERS
Volume 23, Issue 14, Pages 6386-6392

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.nanolett.3c01100

Keywords

peptides; nanofibrils; reassembly; disassembly; cell-cell interactions

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Nature regulates cellular interactions through cell-surface molecules and plasma membranes. Researchers have successfully assembled peptide nanofibrils on live cell surfaces to enhance cellular interactions. Surprisingly, reducing the thermal stability of the nanofibrils promoted cellular interactions, and the study highlights the potential of thermally less stable nanoassemblies in designing functional materials.
Nature regulates cellular interactionsthrough the cell-surfacemolecules and plasma membranes. Despite advances in cell-surfaceengineering with diverse ligands and reactive groups, modulating cell-cellinteractions through scaffolds of the cell-binding cues remains achallenging endeavor. Here, we assembled peptide nanofibrils on livecell surfaces to present the ligands that bind to the target cells.Surprisingly, with the same ligands, reducing the thermal stabilityof the nanofibrils promoted cellular interactions. Characterizationsof the system revealed a thermally induced fibril disassembly andreassembly pathway that facilitated the complexation of the fibrilswith the cells. Using the nanofibrils of varied stabilities, the cell-cellinteraction was promoted to different extents with free-to-bound cellconversion ratios achieved at low (31%), medium (54%), and high (93%)levels. This study expands the toolbox to generate desired cell behaviorsfor applications in many areas and highlights the merits of thermallyless stable nanoassemblies in designing functional materials.

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