Knowledge Base
Quality Control
Becoming and being a FIDA user
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.

Additionally, aggregation is linked to the formation of disease-related aggregates, as seen in neurodegenerative disorders like Alzheimer's disease. In LLPS (Liquid-Liquid Phase Separation), aggregation refers to the process in which specific biomolecules undergo demixing, resulting in the formation of distinct liquid phases within cellular compartments. These phases, known as condensates or membraneless organelles, play crucial roles in organizing cellular components and processes, facilitated by weak, reversible interactions among the molecules involved. LLPS is essential for various cellular functions, including cellular signaling, gene regulation, and stress responses. FIDA is commonly used in LLPS research. See our literature base of application notes and publications on the topic.