NIT Rourkela scientists uncover sugar–protein link to advance bone regeneration technology
New Delhi: National Institute of Technology (NIT) Rourkela, Researchers have uncovered how natural sugar-like molecules in the human body can alter the behavior of Bone Morphogenetic Protrin-2 (BMP-2), a protein responsible for bone formation and repair.
Published in the prestigious journal Biochemistry, the findings of this research can be used for advanced treatments in bone and cartilage regeneration, improved implants, and more effective protein-based medicines.
From building tissues, and supporting chemical reactions, to acting as signals between cells, proteins carry out various functions in the human body. However, for best productivity, they need to be folded or unfolded into precise three-dimensional shapes. Understanding why and how proteins unfold is a major goal in biology, with implications for medicine, biotechnology, and drug delivery.
In this context, BMP-2 plays a crucial role in forming bones and cartilage, healing injuries, and guiding stem cells to become bone-forming cells. However, in the human body, this protein interacts with different Glycosaminoglycans (GAGs), special sugar-like molecules found in connective tissues and joint fluids.
The NIT Rourkela research team led by Prof. Harekrushna Sahoo. Department of Chemistry, National Institute of Technology, Rourkela, along with research scholars Mr. Devi Prasanna Behera and Ms. Suchismita Subadini, investigated how these different GAGs affect BMP-2 when it is exposed to “stress” in the form of urea-induced chemical denaturation.
The team observed that BMP-2 unfolded faster in the presence of Sulfated Hyaluronic Acid (SHA), a type of GAG, compared to regular Hyaluronic Acid or without additives. The researchers found that SHA binds directly to BMP-2 protein, gently altering its structure and making it unfold in a more controlled manner.
Speaking about the findings and potential real-world impact of this research, Prof. Harekrushna Sahoo, said. “BMP-2 is a critical protein in humans that plays a fundamental role in osteogenesis and bone regeneration, residing within the glycosaminoglycan-rich extracellular matrix environment of bone tissue. Our study reveals how specific GAG–BMP-2 interactions influence unfolding dynamics and structural stability. These insights allow scaffold designs to actively preserve BMP-2’s functional conformation, prolong bioactivity, lower dosage needs, and reduce side effects. Furthermore, the work offers a mechanistic basis for tailoring GAG functional group modifications to modulate protein structure and activity, guiding next-generation pharmaceutical formulation.”
BMP-2 naturally exists in vivo and predominantly as part of a proteoglycan complex; consequently, its interactions with GAG chains are integral to its conformational dynamics. These interactions critically influence the protein’s osteoinductive potential. Functional group modifications of GAGs. such as targeted sulfation. can profoundly modulate these interactions, imparting enhanced structural stability under physicochemical stress while preserving bioactivity.
This high-resolution molecular understanding underscores the potential to engineer GAG modifications that not only maintain BMP-2 functionality under adverse conditions but also optimise its therapeutic delivery, augment bioactivity through strategic sulfation or other functional group alterations, and extend protein shelf life via improved stabilisation strategies.
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