We present a systematic study of several factors that influence the stability of Aβ42 fibrils following in silico mutation
2010
Scholarcy highlights
- To design therapeutic agents to combat the progression of Alzheimer’s disease, it is worthwhile to understand the thermodynamics of destabilizing these aggregates and the features that contribute to their stability
- We present a systematic study of several factors that influence the stability of Aβ42 fibrils following in silico mutation
- Results indicate that a finite level of hydration around the Asp23−Lys salt bridge is crucial to protofibril stability, while mutation of Phe to glycine has no effect on the binding free energy of the terminal peptide
- Packing between Ile and the aliphatic portion of the Lys side chain serves to regulate the level of hydration in the core of the protofibril and rigidify the Asp23−Lys salt bridge
- Two additional figures are provided, the first showing the force vs time plots using different pulling rates and the second illustrating the evolution of side-chain contacts as the different protofibrils undergo β-strand twisting over time
- The Role of Molecular Simulations in the Development of Inhibitors of Amyloid β-Peptide Aggregation for the Treatment of Alzheimer’s Disease
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