Dynamics Study of the Self-assembly of an Amphipathic Heptapeptide and Its Application as Glucosidase Mimetic

Controlled peptide assembly is an important approach for the synthesis of materials with diverse functions, which opened up new frontiers in polymer science. Herein, we have qualitatively evaluated the morphological changes of the self-assembly heptapeptide Fmoc-AEAEAEA-CONH2 under various experimental conditions by transmission electron microscopy. The results showed that the morphology of the self-assembled heptapeptide were found to be strongly influenced by the temperature, pH and solvents. And the heptapeptide can form two assemblies, nanofibers and cubes, depending on the kinetic parameters during the fabrication. It was concluded that the rebalance of molecular interactions such as hydrophobic interactions, hydrogen bonding and electrostatic interactions between peptides are responsible for the conversion of morphology. Additionally, the two assemblies could be utilized as the beta-glucosidase mimics, and the catalytic activity of the hydrolases mimics followed the density of active sites outside the assemblies. This finding provided a new perspective to understanding the process of self-assembling and the potential relationship between block architectures and the generation of efficient artificial enzymes.

Automated summary

Controlled peptide assembly is an important method for synthesizing materials with diverse functions in polymer science. The morphology of the self-assembled heptapeptide Fmoc-AEAEAEA-CONH2 was found to be strongly influenced by experimental conditions such as temperature, pH, and solvents. The heptapeptide can form nanofibers or cubes depending on the kinetic parameters during fabrication. The rebalance of molecular interactions, such as hydrophobic interactions, hydrogen bonding, and electrostatic interactions, is responsible for the morphological conversion. The two assemblies can also function as beta-glucosidase mimics, with their catalytic activity following the density of active sites outside the assemblies.