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Protein analysis and characterisation
Protein stability and storage

What is protein aggregation?

Aggregation in molecular biology refers to the degradation process by which biomolecules, such as proteins or nucleic acids, cluster together, often forming larger complexes. After synthesis, proteins typically fold into a particular three-dimensional conformation (native state). This folding process can be impaired, creating protein misfolding or unfolding and lead to the protein aggregate.

It is a phenomenon of particular concern in experimental settings due to its potential impact on protein sample stability, where aggregated proteins can lead to loss of solubility and compromised experimental outcomes. In general, aggregation can be the result of various interactions, including hydrophobic, electrostatic, or van der Waals forces, which puts emphasis on good Quality Control practices.

In other words, protein aggregation refers to the process in which proteins misfold or unfold and subsequently clump together to form larger structures called aggregates. This phenomenon can occur due to various factors such as changes in environmental conditions (pH, temperature,  ionic strength), mutations in the protein sequence, or interactions with other molecules. When proteins aggregate, they often lose their normal functional structure and may become insoluble.

Protein aggregation is associated with numerous diseases, including neurodegenerative disorders like Alzheimer's disease, Parkinson's disease, and Huntington's disease. In these conditions, specific proteins misfold and aggregate, forming toxic aggregates that accumulate in the brain and contribute to neuronal damage and cell death. Understanding the biophysical  mechanisms underlying protein aggregation is crucial for developing strategies to prevent or treat diseases associated with protein misfolding and aggregation.