Protein aggregation or protein aggregation or protein clumping is a biological phenomenon that lies in a protein formation error that results in aggregation, meaning the accumulation of protein clumps, either inside or outside cells. 2. The aggregation of these proteins often results in a harmful toxic effect, meaning that the aggregation of these proteins may appear in a large group of diseases known as amyloidosis, including other diseases such as amyotrophic lateral sclerosis, Alzheimer's, Parkinson's, and Brion's disease. 3 During the stages of protein synthesis, folds occur that make the formed protein a three-dimensional structure and become biologically active only when formed in that form. The folding stage in the process of protein formation occurs due to the repellent property of water molecules. The presence of parts of the protein that are attractive or loving and parts that are repellent or repellent is a reason for the protein to be in its biological state so that the outer part of the protein becomes attractive to water and the inner part repels water. However, some misfoldings may occur during the process of protein formation or misfoldings in a previously manufactured protein in an impromptu accident. In such cases, the cell may not be able to help refold the protein to its normal shape or may not be able to disassemble the previously defective protein, so it begins to clump inside it. During this process, the water-repellent part of the protein becomes exposed and interacts with repulsive parts of other defective proteins, and thus these proteins clump together. Protein clumping can occur for several reasons. Some people may have genetic mutations that make them more susceptible to misfolding during protein formation and make it prone to clumping. In contrast, a defect in the process of refolding the defective protein known as or a defect in the disassembly of the defective protein can lead to protein clumping. It seems that many diseases are accompanied by protein clumping with age, as the cell becomes less able to filter out defective proteins and thus they clump. It is worth mentioning that there are several new studies that assume that protein aggregation is a second step by the cell as a response to the imbalance in the protein cycle. Away from harm or mere coincidence, there has been a pioneering study that has shown that the aggregation of proteins that are clumped due to errors in their folding or their high tendency to aggregation occurs in an organized process by the cell and are placed in specific places for them, and this depends on the quality of the parts that control the repair of these damages, including the HSP and the co-chaperone. In addition, it has been shown that eukaryotic cells have the ability to sort damaged proteins into two separate groups based on the quality of control. 1- The control group in the quality of the nucleolar juxta-nucleolar 2- The control group in the insoluble protein deposit. The existence of two separate groups is due to the existence of two different ways of dealing and interacting with different types of misfolded and clumped proteins. The second type of control group acts as a site for the aggregation of non-objectin proteins such as huntingtin protein. Under difficult conditions such as high temperature, the cellular work of quality control becomes unable to keep up with the work, so the observable protein begins to aggregate into the first control group, which is the juxtanuclear group, and eventually begins to disintegrate, which means that the aggregation is an organized and controlled process by the cell. According to one theory, protein aggregation is a cause of aging, and this theory may seem testable given that there are ways to delay aging. Therefore, if the increase in protein aggregation is not related to aging, then slowing down the aging process will not result in any change in the rate of collateral damage of protein aggregation over time. However, aging is associated with a decline in the protection system from protein aggregation damage. To solve the problem, different methods were found to examine the toxicity of protein aggregation in C-elegans. Through these studies, it was shown that reducing the work of one of the most important regulatory pathways, including insulin growth factor signaling 2S, may result in protection from neurodegeneration associated with the toxicity of the aggregated protein. The validity of this approach has been demonstrated in mammals by reducing the regulatory pathway in insulin growth factor-1 activity, which resulted in greater protection from Alzheimer's disease in mice in terms of behavior and the organic chemistry associated with the defect in the disease. Although there is an idea that the aggregation of fully formed proteins may be toxic, new research has shown that incomplete and clumped proteins are more toxic. The hydrophobic parts of these clumped proteins may cause interaction with other components of the cell and cause damage to them. One theory about how cellular damage occurs by clumped proteins suggests that it occurs due to disruption of the cell wall. It is known that clumped proteins in laboratory tubes are able to destabilize the manufactured lipid bilayer, which is similar to that found in living cells, thus leading to increased disintegration of the cell wall.