Abstract
Understanding the structure-morphology relationships of self-assembled nanostructures is crucial for developing materials with the desired chemical and biological functions. Here, phosphate-based naphthalimide (NI) derivatives have been developed for the first time to study the enzyme-instructed self-assembly process. Self-assembly of simple amino acid derivativeNI-Ypresulted in non-specific amorphous aggregates in the presence of alkaline phosphatase enzyme. On the other hand,NI-FYpdipeptide forms spherical nanoparticles under aqueous conditions which slowly transformed into partially unzipped nanotubular structures during the enzymatic catalytic process through multiple stages which subsequently resulted in hydrogelation. The self-assembly is driven by the formation of beta-sheet type structures stabilized by offset aromatic stacking of NI core and hydrogen bonding interactions which is confirmed with PXRD, Congo-red staining and molecular mechanical calculations. We propose a mechanism for the self-assembly process based on TEM and spectroscopic data. The nanotubular structures ofNI-FYpprecursor exhibited higher cytotoxicity to human breast cancer cells and human cervical cancer cells when compared to the nanofiber structures of the similar Fmoc-derivative. Overall this study provides a new understanding of the supramolecular self-assembly of small-molecular-weight hydrogelators.
Original language | English |
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Number of pages | 11 |
Journal | Chemistry - An Asian Journal |
DOIs | |
State | E-pub ahead of print - 11 Jul 2020 |
Keywords
- Supramolecular chemistry
- Naphthalimide
- Peptide
- Enzyme catalysis
- Hydrogel
- NANOSTRUCTURES
- EMISSION
- FIBRILS