PerspectiveBiochemistry

Visualizing Amyloid Assembly

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Science  20 Apr 2012:
Vol. 336, Issue 6079, pp. 308-309
DOI: 10.1126/science.1220356

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Summary

Ordered amyloid fibril protein aggregates are a hallmark of a class of human diseases that includes Parkinson's and Alzheimer's. How proteins assemble into these structures is poorly understood (1) but is thought to play a direct role in disease. Two recent studies provide key insights into this problem. On page 362 of this issue, Neudecker et al. (2) have visualized the changes that convert a normally soluble protein into an aggregation-prone amyloid precursor. Laganowski et al. (3) have described the structure of a subsequent oligomeric amyloid intermediate of the kind currently believed to be responsible for amyloid-associated toxicity (4).