Amino acid functionalized fullerenols: synthesis and applications in enzyme mimicry and organocatalysis

Date

2025-3-6

Author

Dolgun, Volkan

Metadata

Show full item record

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Item Usage Stats

40
views

0
downloads

Cite This

Buckminsterfullerene (C60) and its derivatives, particularly fullerenol, have gained attention due to their versatile applications. Fullerenol is hydrophilic and can be easily functionalized, making it a promising scaffold for catalysis. Amino acid-functionalized fullerenols tend to aggregate and form enzyme-like structures known as ‘fullerenzymes,’ which mimic enzymatic activity and serve as catalysts in organic reactions. In the first part of this study, arginine functionalized fullerenol (F-Arg) was used as a biomimetic catalyst for LarE, the sulfur insertase of lactic acid racemase (Lar) from Lactobacillus plantarum. F-Arg facilitated the conversion of cysteine and nicotinic acid derivatives in buffer solution, mimicking the enzymatic transformation to dehydroalanine. In the second part, histidine and serine functionalized fullerenol (F-HS) was coordinated with nickel ions and investigated as an esterase-mimic for acetylcholine detection in human serum. The F-HS-Ni sensor exhibited high sensitivity and selectivity, demonstrating its potential for biomedical applications. In the third part, fullerenols and their amino acid derivatives were explored as organocatalysts. They efficiently catalyzed carbon dioxide fixation under mild conditions. Additionally, F-Arg served as basic catalysts in the Morita-Baylis-Hillman reaction and chromene synthesis. Fullerenols were also used as Brønsted acid catalysts in the Prins reaction. These findings highlight the potential of fullerenol-based catalysts in biomimetic and organic transformations.

Subject Keywords

Fullerene, Enzyme mimics, Sulfur insertase, Organocatalysis, Alzheimer’s disease

URI

https://hdl.handle.net/11511/114096

Collections

Graduate School of Natural and Applied Sciences, Thesis