Preliminary Programme

For this advanced course, six highly relevant and related topics have been selected:

1. Amyloid structures: Recent structural analysis suggests a molecular basis for amyloid polymorphism and alternative concepts for amyloid formation.
2. Chaperones in amyloid formation: Molecular chaperones are an important cellular target to control pathogenic amyloid formation and possibly amyloid clearance. 
3. Membrane-less organelles: Membrane-less compartments in cells (LLPS) may promote protein fibrilization in neurodegenerative and related diseases.
4. Lipids and membranes in amyloid formation: Lipids/lipid membranes provide a hydrophobic surface which can catalyze the formation of amyloid(like) structures.  
5. Functional amyloids: Functional amyloids reinforce the emerging concept that the amyloid fold is capable of carrying out a diversity of (biological) functions.
6. Pathology of amyloids: Amyloids are observed in neurodegenerative and age-related diseases. The molecular basis for toxicity of amyloids is poorly understood.

Schedule

Speakers Lecturers

• Biomolecular condensates at the nexus of stress, disease and ageing

• Chaperone action on amyloids

• Alpha-Synuclein fibril strains: ​​​​​​​Decoding Strain Transformations and their possible role in Parkinson's disease.
• (Dis)functional membrane interactions of the intrinsically disordered protein alpha-synuclein.

• Intrinsically disordered proteins as drug targets
• Interactions and regulation of disordered proteins

• Cellular landscapes of protein interactions.
• Sequence-based determinants of aggregation within protein condensates.

• Lipid changes associated with alpha-synuclein and Parkinson’s Disease pathology
• Strategies to prevent and revert apha-synuclein aggregation and lipid changes associated with Parkinson’s Disease

• Regulation of autophagy by lipid-mediated protein oligomerization

• Biophysical principles of chaperone-client interactions resolved at the atomic level
• Regulation of dynamic chaperone interactions networks and functional cycles

• Biophysical approaches to study molecular mechanisms of Alzheimer’s disease that involve lipids
• Molecular mechanism of Alzheimer’s disease: towards drug development

•  Cooperative biniding of α-synuclein to membranes. Mechanism of membrane-induced α-synuclein aggregation and the associated protein-lipid co-aggregation
  

• Engineering the self-assembly of functional amyloids; from the molecule to hydrogel for healthcare applications

•  Proteostasis Collapse in Aging and Neurodegenerative Disease

• Functional amyloids in bacteria: mechanisms and microbiology
• Pathological protein oligomers in conformational diseases

• Seeing amyloid: beautiful structures and toxic mechanisms

• Heterotypic Amyloid interactions and their effect on amyloid assembly
• Evolutionary imprints of protein aggregation on protein structure and chaperone interactions

• The cellular protein folding machinery
• Chaperone control of Tau fibrils

• Structure determination of amyloids by helical reconstruction of cryo-EM images
• Cryo-EM structures of tau filaments in neurodegenerative disease

• Protein Folding 2.0: How molecular chaperones reverse and protect against amyloid aggregation
• The diverse nature of functional amyloids: from bacteria to humans.