Latest news with #BoneMorphogeneticProtein-2
Time of India
2 days ago
- Health
- 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.
India Today
4 days ago
- Health
- India Today
NIT Rourkela study cracks protein puzzle for stronger bone repair
Researchers at the National Institute of Technology (NIT) Rourkela have found how certain natural sugar-like molecules in human body can change the way a key bone protein behaves. The work, published in the journal Biochemistry, offers clues for improving bone and cartilage repair treatments, designing better medical implants, and developing more effective protein-based are workhorses in the human body, building tissues, carrying signals, and supporting chemical reactions. For these roles, proteins must fold into specific three-dimensional in their structure can affect how well they work. Understanding how and why a protein unfolds is a long-standing challenge in biology, with applications ranging from drug delivery to tissue ROURKELA MAPS SUGAR-PROTEIN LINK FOR BETTER BONE REPAIR METHODS The study focused on Bone Morphogenetic Protein-2 (BMP-2), a molecule central to bone and cartilage formation. BMP-2 also helps stem cells turn into bone-forming cells and supports healing after the body, BMP-2 operates in an environment rich in glycosaminoglycans (GAGs), sugar-like molecules found in connective tissue and joint fluids. The NIT Rourkela team, led by Professor Harekrushna Sahoo from the Department of Chemistry, examined how different GAGs affect BMP-2 under chemical scholars Devi Prasanna Behera and Suchismita Subadini worked alongside him in the study. The team used urea to induce unfolding and compared the behaviour of BMP-2 with and without results showed that in the presence of Sulfated Hyaluronic Acid (SHA), a type of GAG, BMP-2 unfolded faster than it did with regular hyaluronic acid or without any study suggests that SHA binds directly to BMP-2, altering its structure in a way that makes the unfolding process more Sahoo explained that BMP-2 functions within a GAG-rich environment in bone tissue, and these molecular interactions shape its structure and understanding these interactions, it may be possible to design scaffolds that keep BMP-2 in its active form for longer, reduce the dosage needed in treatments, and limit side research also points to a broader idea, modifying the functional groups of GAGs, such as through targeted sulfation, could help stabilise proteins like BMP-2 under stress without losing their could guide the creation of new drug formulations, extend protein shelf life, and make therapeutic delivery more mapping these detailed molecular relationships, the NIT Rourkela study provides a framework for future work in regenerative medicine, where fine-tuning the environment around proteins can be as important as the proteins themselves.- Ends
