Protein Misfolding Diseases

Large no diseases in humans result from protein misfolding and aggregation. An error in the conformation of protein causes disease. It is believed that the primary cause of Alzheimer’s, Parkinson’s, Huntington’s diseases is protein misfolding.

In medicine, it is called proteinopathies. The protein conformational disorders (neurodegenerative or protein misfolding diseases) of protein folding diseases which include

1.            Creutzfeldt-Jakob disease

2.            Guacharos disease

3.            Cystic fibrosis

4.            Ant diuretic hormone

5.            Endoplasmic reticulum

6.            Heat shock protein

7.            Mad cow disease

8.            Retinitis pigmentosa

9.            Spino cerbrelloataxia

10.          Arginine vasopressin, etc

Protein folding is very essential for the living organism because it adds strength to the gene structure, any error in the folding process cause misfolding to the protein, thereby causing lethal in the cellular system. Furthermore the evidence suggests that the small non-fibril protein aggregates known as oligomers are toxic in the cells of an affected organ.

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Some proteins can be induced to form abnormal structures by exposure to the same protein that has folded into disease-causing confirmation and this process seeding or permissive templating. The best-known forms of inducible proteinopathy are prion diseases which can be transmitted by exposure of a host organism to purified prion protein in a disease-causing confirmation. In all of these instances, an aberrant form of the protein itself appears to be a pathogenic agent. The misfolding is mainly due to high viscosity in the cellular system, many proteins cannot fold themselves in order but require of support of other special chemicals like chaperones. The molecular chaperones assist other proteins to achieve a functionally active 3d structure and thereby preventing the formation of misfolded or aggregated structures and enhancing the folding efficiency by increasing the kinetics in the process and inhibit the aggregation.

The role of chaperones in suppressing the effect of protein misfolding is well explained in various literature. The pharmacological aspects of different chaperones suggest that their uses potential therapeutic agents against different types of degenerative, including neurodegenerative or protein misfolding diseases.