The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth

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• Dr Sanne Abeln, Vrije University Amsterdam
• Wednesday 25 November 2020, 14:30-15:30
• Zoom - link to be announced.

If you have a question about this talk, please contact Lisa Masters.

Most proteins fold in the cell into stable, compact structures. Nevertheless, many proteins also have the ability to stick together, forming long fibrillar structures that are associated with a wide range of human disorders including Alzheimer’s and Parkinson’s disease. The exact nature of the amyloid-causing stickiness is not well understood, nevertheless amyloid fibrils show some very specific thermodynamic characteristics. Some fibrils even destabilise at low temperatures. In this work we translate hydrophobic theory previously used to model protein folding to fibril formation. We combine this theory with experimental measurements, simulations and meta-data analysis and we consider several different types of fibrils. This allows us to unravel the nature of the stickiness in amyloid fibrils. Overall, we show that amyloid fibril elongation is associated with a negative heat capacity, the magnitude of which correlates closely with the hydrophobic surface area that is buried upon fibril formation, highlighting the importance of hydrophobicity for fibril stability.

This talk is part of the Theory - Chemistry Research Interest Group series.

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