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Shapeshifting fibers: capturing the transformation of a rogue protein

Research Highlights

For the first time, an interdisciplinary team of researchers has revealed intricate 3D detail of how the structure of a malfunctioning protein, hIAPP, evolves over time.

Scientists used Cryo-Electron Microscopy (cryoEM) – a high resolution imaging technique - to determine the structures of the hIAPP amyloid fibrils present at three distinct points of growth; an early stage when the first fibrils had formed, an intermediate point where fibrils grow dramatically, and a late time point when the fibrils had reached an apparent steady state.

Remarkably, different fibril polymorphs (various structures of the same protein sequence) were observed at different stages of assembly, with some structures only present at certain times.

In total, seven distinct hIAPP fibril polymorphs were observed as part of the study including five new structures that had not been observed previously at a single reaction time point.

Read the full press release on the Faculty of Biological Sciences website. 

Read Structural evolution of fibril polymorphs during amyloid assembly on the Cell website.