Genomics | Synthetic Biology | Immunology | Reproduction
We show that a few interactions (energetic couplings) between parts of Aβ42 are significant for the nucleation process. These interactions happen at the C-terminus of the protein and are a subset of those found in the final fibril structures from Alzheimer’s patients’ brains.
We show that a few interactions (energetic couplings) between parts of Aβ42 are significant for the nucleation process. These interactions happen at the C-terminus of the protein and are a subset of those found in the final fibril structures from Alzheimer’s patients’ brains.
By tracking how each mutation affected the speed of fibril formation, we built a complete energetic map of the Aβ42 nucleation reaction. We show that mutations in the latter part of Aβ42 (C-terminus / hydrophobic core) are largely disruptive for nucleation.
By tracking how each mutation affected the speed of fibril formation, we built a complete energetic map of the Aβ42 nucleation reaction. We show that mutations in the latter part of Aβ42 (C-terminus / hydrophobic core) are largely disruptive for nucleation.
And yet, it may be the most important step in the disease process, which so far scientists have struggled to study and understand. If we could block nucleation, we might stop Alzheimer’s before it starts 🧠
And yet, it may be the most important step in the disease process, which so far scientists have struggled to study and understand. If we could block nucleation, we might stop Alzheimer’s before it starts 🧠