How Can NIT Rourkela's Study Enhance Bone Regeneration Technology?

New Delhi, Aug 13 (NationPress) Researchers at the National Institute of Technology (NIT) Rourkela have discovered how natural sugar-like molecules within the human body can modify the behavior of a protein vital for bone formation and repair.

The study, featured in the journal Biochemistry, holds potential for advanced therapies in bone and cartilage regeneration, enhanced implants, and more effective protein-based treatments.

Proteins perform a myriad of functions in the human body, from tissue construction and chemical reaction support to serving as cellular signals.

Yet, optimal functionality requires them to be folded or unfolded into specific three-dimensional configurations. Understanding the mechanisms of protein unfolding is a significant focus in biology, impacting medicine, biotechnology, and drug delivery.

In this context, Bone Morphogenetic Protein-2 (BMP-2) is crucial for the formation of bones and cartilage, injury healing, and directing stem cells to differentiate into bone-forming cells, as noted by the NIT research team.

This protein interacts with various Glycosaminoglycans (GAGs), unique sugar-like molecules found in connective tissues and joint fluids.

The researchers explored how these GAGs influence BMP-2 when subjected to “stress” from urea-induced chemical denaturation.

The findings revealed that BMP-2 unfolded more rapidly in the presence of Sulfated Hyaluronic Acid (SHA)—a type of GAG—compared to regular hyaluronic acid or in the absence of additives.

The team discovered that SHA binds directly to the BMP-2 protein, subtly modifying its structure and facilitating a more controlled unfolding process.

“BMP-2 is a vital protein in humans that plays a key role in osteogenesis and bone regeneration, residing within the glycosaminoglycan-rich extracellular matrix environment of bone tissue. Our findings illustrate how specific GAG-BMP-2 interactions affect unfolding dynamics and structural integrity,” stated Prof. Harekrushna Sahoo.

“These insights pave the way for scaffold designs that can actively maintain BMP-2’s functional conformation, extend bioactivity, reduce dosage requirements, and minimize side effects. Moreover, this work provides a mechanistic foundation for customizing GAG functional group modifications to adjust protein structure and activity, guiding next-generation pharmaceutical development,” Sahoo added.

BMP-2 naturally exists in vivo, primarily as part of a proteoglycan complex; thus, its interactions with GAG chains are essential for its conformational dynamics and critically influence the protein’s osteoinductive capacity.

Modifications of GAG functional groups, like targeted sulfation, can significantly alter these interactions, enhancing structural stability under physicochemical stress while preserving bioactivity.

The research findings can assist in crafting enhanced biomaterials and drug delivery systems for treating bone fractures, spinal injuries, and degenerative bone diseases. They can also optimize drug delivery during treatments and mitigate side effects for patients.