Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
Protein aggregation is the process by which misfolded proteins adopt a conformation that cause its polymerization into aggregates and organized fibrils. Many neurodegenerative diseases (amyloidoses) are associated with protein aggregation, though smaller oligomeric forms of the misfolded (amyloidogenic) proteins have been implicated as the causative agent.
Aggregated forms of α-synuclein are characteristic of Parkinson’s disease. Here the authors show that the condensation-driven aggregation pathway of α-synuclein can be inhibited using small molecules: the aminosterol claramine stabilizes α-synuclein condensates and inhibits α-synuclein primary nucleation in the aggregation process.
The aggregation of the neuronal protein α-Synuclein is associated with the onset of Parkinson’s disease. Here the authors report a two-dimensional Fragment Assisted Structure-based technique to find antagonists of α-Synuclein aggregation and show its promise for identifying lead therapeutics for Parkinson’s disease.
Pei et al. applied Gaussian process-based machine learning to capture dynamic spatial covariance relationships managed by proteostasis to mediate cooperative folding on a residue basis as a standard model for precision disease management.
Maintaining a healthy nuclear proteome during DNA damage is important but its regulation is poorly understood. The authors here show that a SUMO modification of the small heat shock protein Btn2 regulates yeast nuclear protein sequestration during stress.
Modulating amyloid protein phase separation and fibrilization may help in addressing neurodegenerative diseases. This study demonstrates that halogen-doped graphene quantum dots can modulate these processes in TDP-43 in both nucleus and cytoplasm.
Claire Durrant reminds us of the importance of studying the physiological roles of proteins and their aggregates to understand their roles in disease and inform therapies, discussing a 2008 paper on amyloid-β from the Arancio lab.
Plants have an additional organelle to animals (the chloroplast), which means that they have a greater repertoire of protein homeostasis (proteostasis) mechanisms. We find that chloroplast proteostasis components prevent aggregation of a pathogenic fragment of human huntingtin expressed in plants, which reveals a potential avenue for therapeutic intervention in human proteinopathies.