Rourkela
How can researchers at the National Institute of Technology (NIT) Rourkela affect the behavior of protein, bone morphonnetic protein-2 responsible for the manufacture and repair of natural sugars found in the human body? It has been detected.
The findings of this research published in the iconic magazine biochemistry can be used in the development of advanced treatment of bone and cartilage regeneration, better implants and more effective protein-based drugs. Proteins do various functions in human body. From the construction of tissue and cooperation in chemical reactions, from cooperation to acting as signs between cells, they play a big responsibility.
However, for best productivity, it is necessary to turn or open accurately in three-dimensional figures. Why and how do proteins open? Understanding this is a major goal of biology. It affects therapy, biotechnology and drug delivery. In this context, BMP-2 plays an important role in building bone and cartilage, correcting injuries and transfering stem cells into bone-making cells.
However, this protein in human body processes with molecules such as various glycosaminoglycities (GAG), connective tissues and special sugars found in the liquids of joints. Prof. of Chemistry Department of NIT Rourkela’s research team. This research was done under the guidance of Harekrishna Sahu. In this, research scholar Devi Prasanna Behera and Suchismita Subadini had an important participation.
He researched how various GAGs affect BMP-2, when urea-inspired chemical deanchurations fall into ‘stress’. The team noticed that BMP 2 opens rapidly than normal hyaluronic acid or no additives in the presence of a type of CAG – sulfed hyaluronic acid (SHA). Researchers found that SHA directly connects to BMP-2 protein, its structure gradually changes and helps to open it with more control.
Pro. Harekrishna Sahu explained the findings of this research and the potential real benefits from it that BMP-2 is an important protein found in humans. This bone plays a basic role in the manufacture and reconstruction of bones by being present in external mechanical matrix rich in glycosaminoglycan of tissue.
Our research indicates how special interactions between GAG-BMP-2 affect the activity and structural stability. With this understanding, scaffold design provides competence to protect the compatibility of BMP-2, to increase bioactivity, reduce dosage and reduce side effects. Along with this, this task gives a mechanical basis for the adaptation of the amendments of the GAG functional group for the protein structure and modulation of activity, which becomes the guide to the creation of the next generation of medicines.
BMP-2 is naturally present in organisms and mainly as part of a protiology complex. As a result, its mutual processes with GAG chains are an integral part of its compatibility activity.
These mutual processes severely affect protein osteoondractive capacity. Amendment to the functional group of GAG such as targeted sulfation can depth such interpretation processes, resulting in physical-chemical stress also leads to better structural stability as well as bio-activation.
This high-resolution molecular understanding underlines the possibility that GAG amendments can be engineered in such a way that not only maintains the functionality of BMP-2 in adverse conditions, but adapt to its medical distribution. Increase biodiversity through strategic sulfation or other functional group changes and also increase the shelf life of protein by advanced stabilization strategies.
