Multidimensional Structure–Activity Relationship of a Protein in Its Aggregated States

The same, but very different: Diverse chemical, physical, and biological conditions induced the aggregation of a single protein into five structurally distinct protein aggregates (see electron micrographs, scale bars: 500 nm), all of which contained the cross-β-sheet motif. The aggregates differed in their affinity for adenosine-5′-triphosphate, thioflavin T, DNA, and membrane mimics, and in their interference with cell viability.