Recreating the complex and precise functions of natural enzymes through artificial means has been one of the formidable challenges in science. Enzymes, which catalyse several vital biochemical reactions in living organisms, possess unmatched specificity, efficiency and biocompatibility.

Replicating these qualities in artificial enzymes has been a significant hurdle, particularly in ensuring that they function as effectively as enzymes without hindering other biochemical processes.

Artificial enzymes

Researchers at the CSIR-Central Leather Research Institute (CSIR-CLRI), Chennai, have made significant achievements in nanozymes (nanomaterials that function like enzymes), unveiling innovative approaches that could transform the field of artificial enzymes and the development of collagen-based biomaterials.

Two studies from Dr Amit A Vernekar’s research group, recently published in Chemical Science, highlight their pioneering work in expanding the field of artificial enzymes.

The first study focuses on a manganese-based oxidase nanozyme (MnN) that presents significant potential in the biomedical field. This MnN nanozyme, as described by the first author Adarsh Fatrekar, can activate collagen, a major structural protein, and neatly crosslink its tyrosine residues using only a trace amount of tannic acid. “Our work shows that this process maintains the collagen’s natural triple-helical structure, which is vital for its function in medical applications,” says Fatrekar.

Traditional methods of crosslinking collagen often involve harsh chemicals or extreme conditions, which can lead to toxicity or denaturation of the protein. However, the CLRI team has showed that the nanozyme can function under mild conditions too, ensuring that the collagen retains its structural integrity while offering high resistance to enzymatic degradation. This breakthrough is of high significance for creating durable and stable collagen-based biomaterials for wound healing, tissue engineering and several other medical uses.

Vernekar emphasised the importance of this discovery as thus: “Our research expands the role of nanozymes beyond their conventional uses with small molecules, bridging a crucial gap in the field. This development not only enhances our understanding of nanozymes’ chemistry but also paves the way for the development of new, safer and more effective biomaterials.”

The study reveals that the MnN nanozyme confers remarkable resistance to collagenase, an enzyme that typically degrades collagen, by forming a tannic acid-tyrosine linkage that likely hinders collagenase’s ability to recognise and break down the protein.

Precision medicine

In another related study, Dr Vernekar’s research group has explored how biomolecules interact with the enzyme-like catalytic sites within a metal-organic framework. This research highlights the importance of controlling these interactions, which is crucial for the effectiveness of artificial enzymes in medical applications.

“By recreating enzyme-like activity in the pockets of the metal-organic frameworks, we were able to manage how biomolecules interact in ways that conventional methods can’t achieve. This opens up new possibilities for creating more precise artificial enzymes having lesser side reactivities,” explains the first author, Rasmi Morajkar, a DST-Women in Science and Technology (WISE) PhD fellow.

Together, these studies mark a significant step forward in the field of nanozyme research for developing the next-generation of artificial enzymes.

As the team continues to push the boundaries of nanozyme technology, their work promises to bring about safer, more efficient solutions for biomedical applications, particularly in the development of collagen-based biomaterials.





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