Protein drug stability is gaining importance in drug therapy
Protein stability is an important factor. It depends on the net balance of forces the position of protein to be in its native folded conformation or unfolded or extended state. The stability of a protein is very small. Hence, protein-drug stability is crucial when recombinantly expressed proteins are crucial to assess how the properties affect the drug value, their side effects, and the ability of the protein to survive for a longer period. Protein is the main brick for building the body that enables the body to fight all diseases. It is important to identify and characterize protein that empowers the experts with a thorough knowledge of the disease and the post-translational modification that can handle and alter the behavior of the protein.
Protein that brings out toxic
Chemists of MIT, with their in-depth study, have discovered that the structure of a protein can pump out the toxin part of the bacterial cell.
- The study of proteins drug resistance is similar to one found in E.Coli, which helps the bacteria be resistant to several antibiotics.
- With the help of NMR or Nuclear magnetic resonance, the researchers can determine how the structure of protein changes when the molecule of the drug moves through it.
- Once the knowledge of the structure is known to the researchers, they can design the drugs that will block the transport proteins and again sensitize the drug-resistant bacteria to the existing antibiotics.
Factors for the process of protein folding :
- Conformational and compositional stability
- A cellular environment like its temperature and pH
- Primary and secondary structure
- Hydrogen bonding
- Solvation
- Salt bridges
- Hydrophobic effect
- Ligand binding
- Cofactor binding
Allosteric regulation
Essentially the disordered protein is predominant in allosteric regulation. Earlier it was thought that essential disorder is for maximizing the allosteric coupling and hence the proposal of a comprehensive ensemble model to compare the role of order-order transition and disorder-order transition in the Ensemble allosteric model. With such a fact, it is revealed that order-order transition has a higher chance than a disorder-order transition in allostery.
The allosteric effect is an important mechanism of regulation in the biological process that binds the ligand on one side of the protein and influences the function of the distant site.
Final note
Protein storage for protein stability, conformation, and activity. They are the main element that fights all kinds of diseases, and a sudden change in the environment leads to protein degradation, and precipitation, and these are mostly irreversible. It is essential to understand the behaviour and nature of the protein before developing the test for its purification.
Protein stability relies greatly on the storage of pH that is provided by the buffer. Hence it is important to provide the right pH environment for optimum stability.
