Mysteries of protein oligomers in the article published by University of Tehran researchers in the journal affiliated with Cambridge University

According to the public relations report of University of Tehran, Dr. Ali Akbar Mousavi Movahedi, the Dean of Institute of Biochemistry and Biophysics (IBB), said about this: The change in lifestyle in today's world has imposed various tensions and stresses on the individual and social health of humans. It has also led to the increasing number of people suffering from industrial diseases such as diabetes and cancer.

Many studies have confirmed the essential role of the production and release of free radicals as a result of these tensions in the occurrence of diseases.

Although the system of creation has provided the necessary mechanisms to deal with such tensions by creating balance in the body of living beings up to a certain threshold.

However, the dramatic increase in stress in today's industrial life pushes the established balance in favor of the accumulation of free radicals in the body, which can impose adverse changes on the structure and function of biological molecules, including proteins.

He reminded that the molecular root of stress or tension is related to the accumulation of unbalanced free radicals, which causes structural changes and destabilization of proteins, leaving them out of their normal state, placing them in cumulative pathways and eventually causing diseases such as Alzheimer's, Parkinson's and becomes diabetes; He added: In these diseases, the deposition of protein accumulations known as amyloid fibrils leads to disturbances in the normal functioning of the body's organs, for example, the destruction of pancreatic beta cells due to the deposition of amyloid fibrils affects insulin secretion and leads to type 2 diabetes.

Professor of University of Tehran noted: Also, the role of amyloid fibril deposition in nerve cells has been proven in the development of progressive neurological diseases such as Alzheimer's and Parkinson's, but the matter is much more complicated from the molecular point of view; because many studies do not consider the toxicity of amyloid fibrils, which are considered the final product of protein aggregation processes, to the extent that they are solely responsible for causing the aforementioned diseases. Therefore, recently, the discussion of amyloid oligomers, which are intermediates and precursors of protein aggregation pathways and have much more toxicity than fibrils, has attracted a lot of attention.

Prof. Mousavi Movahedi added: Since toxic amyloid oligomers are completely separate from protein oligomers due to their low thermodynamic stability and special molecular structures, which carry the main burden of biological operations, they are the main candidates for causing disruption and ultimately destroying cells and causing industrial amyloid diseases. They are mentioned above. Due to the high importance of this issue, the researchers of the Institute of Biochemistry and Biophysics (IBB) of University of Tehran, at the invitation of the journal Current Research in Structural Biology affiliated with the University of Cambridge, England, published a review article in which, while examining the pathways of protein aggregation and the mechanisms involved in it, the methods  ,they have also described the management of these conditions in living organisms.

He added: Therefore, in this review article that focuses on structural aspects, the mysteries of protein oligomers have been revealed, and the main emphasis is on two groups of protein oligomers known as amyloid oligomers and molecular chaperones, the first group threatening the cell and the second group (by managing stressful conditions) are considered the guarantor of cell health. It should be mentioned that the molecular mechanisms involved in the above cases have been drawn by the authors of the article and published in this article.