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


  • We thank Dr. S. Choe, Dr. L. Goldschmidt, Dr. E. Evangelisti, Dr. C. Cecchi, Dr. P. Arosio, and Dr. M. Morbidelli for experimental assistance and discussions. This research was supported by the Swiss National Science Foundation.


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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.

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