Enzyme Instructed Self-assembly of Naphthalimide-dipeptide: Spontaneous Transformation from Nanosphere to Nanotubular Structures that Induces Hydrogelation

Rajan Deepan Chakravarthy, Mohiuddin Mohammed, Hsin-Chieh Lin*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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 languageEnglish
Number of pages11
JournalChemistry - An Asian Journal
StateE-pub ahead of print - 11 Jul 2020


  • Supramolecular chemistry
  • Naphthalimide
  • Peptide
  • Enzyme catalysis
  • Hydrogel

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