Amyloids & protein aggregation

How do proteins assemble into amyloid structures, and what happens when different amyloids meet?

Why amyloids matter

Amyloids are ordered protein assemblies with a characteristic cross-β structure. They are studied in the context of protein misfolding and disease, but they also have biological functions: bacterial curli, for example, contribute to the extracellular matrix of biofilms. Understanding amyloids means looking at both their molecular structure and the biological setting in which they form.

Aggregation is also an interaction problem. One protein can alter the aggregation of another, and the outcome depends on the proteins, experimental conditions and the measurements used. Bringing those observations together makes it easier to compare findings that would otherwise remain scattered across the literature.

Questions we explore

How can we organise evidence about interactions between different amyloid-forming proteins?
What makes an amyloid dataset useful for prediction and comparison?
How can computational predictions and experimental measurements inform each other?

Our approach

We connect literature curation, databases, computational analysis and experimental evidence. AmyloGraph organises reports of amyloid–amyloid interactions, while our work on prediction and annotation examines how reliably sequence-based models describe amyloid behaviour.

We also study the resources and experimental methods used across the field. Clear annotations and complementary measurements help distinguish an observed interaction from a proposed mechanism. Our publication stories below explain the questions, methods and limitations behind these projects.