A guide to studying protein aggregation

Disrupted protein folding or decreased protein stability can lead to the accumulation of (partially) un- or misfolded proteins, which ultimately cause the formation of protein aggregates. Much of the interest in protein aggregation is associated with its involvement in a wide range of human diseases and the challenges it poses for large-scale biopharmaceutical manufacturing and formulation of therapeutic proteins and peptides. On the other hand, protein aggregates can also be functional, as observed in nature, which triggered its use in the development of biomaterials or therapeutics as well as for the improvement of food characteristics. Thus, unmasking the various steps involved in protein aggregation is critical to obtain a better understanding of the underlying mechanism of amyloid formation. This knowledge will allow a more tailored development of diagnostic methods and treatments for amyloid-associated diseases, as well as applications in the fields of new (bio)materials, food technology and therapeutics. However, the complex and dynamic nature of the aggregation process makes the study of protein aggregation challenging. To provide guidance on how to analyse protein aggregation, in this review we summarize the most commonly investigated aspects of protein aggregation with some popular corresponding methods.

Automated summary

Disruptions or instabilities in protein folding can lead to the accumulation of misfolded proteins and the formation of protein aggregates, which are associated with human diseases and pose challenges in biopharmaceutical manufacturing. However, protein aggregates can also be functional and have applications in biomaterials, therapeutics, and food improvement. Understanding the steps involved in protein aggregation is crucial for developing diagnostic methods, treatments, and applications in various fields. The study of protein aggregation is challenging due to its complex and dynamic nature.