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Time of India

NIT Rourkela decodes sugar molecules, protein complex to boost bone regeneration tech

New Delhi: Researchers at the National Institute of Technology (NIT), Rourkela have uncovered how natural sugar-like molecules in the human body can alter the behaviour of Bone Morphogenetic Protein-2 (BMP-2), a protein responsible for bone formation and repair, according to officials. 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. According to Harekrushna Sahoo, Associate Professor, NIT, Rourkela, proteins carry out various functions in the human body -- from building tissues and supporting chemical reactions to acting as signals between cells. However, for the 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," Sahoo said. 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. "BMP-2 is a critical protein in humans that plays a fundamental role in osteogenesis and bone regeneration . 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," he said.