Strategies and tools for modulating

pathologic protein self-assembly


March 21-22, 2019 | Instituto de Investigação e Inovação em Saúde - i3S, University of Porto, Portugal



The workshop on “Strategies and tools for modulating pathologic protein self-assembly"  will join leading experts to discuss the current knowledge on the mechanisms underpinning self-assembly of disease-related proteins and present strategies to modulate toxic protein aggregation. Aberrant protein self-assembly is linked to over 30 human disorders, including neurodegenerative diseases, type-2 diabetes, and systemic amyloidosis. Misfolded and aggregated proteins also play a detrimental role in conditions in which clearance becomes deficient, such as lysosomal storage diseases. In addition, amyloid structures can be hijacked by viruses, e.g. HIV to increase infection. In all these conditions, a common characteristic of the proteins involved in the appearance of diverse, mostly non-native assemblies of the disease-related proteins, ranging from small oligomers to amyloid deposits. We have recently witnessed significant progress in understanding the biophysical and structural properties of these protein assemblies and in identifying their cytotoxicity mechanisms. These advances have been crucial to developing novel disease-modifying strategies and molecules. Despite this significant progress, we are still waiting for the appearance of the first effective drug designed to abrogate pathological protein self-assembly.
The advances in the field and discussion of future research paths presented in this workshop will provide a collection of articles that will be compiled in a Research Topic to be published in Frontiers in Molecular Neuroscience. We encourage the submission of innovative perspectives, reviews and original research articles on this topic that will contribute to stimulate the discussion of novel therapeutic avenues to tackle a significant number of severe human diseases.








21st March 2019


9:00 - 9:30 Registration



Co-organized by COST BM1405 NGP-net


9:30-9:40 Welcome


9:40-10:10 The structural determinants of protein oligomer toxicity and strategies for their neutralization | Fabrizio Chiti, Italy

10:10-10:30 An integrated bacterial discovery platform for chemical rescuers of disease-associated protein misfolding and aggregation | Georgius Skretas, Greece

10:30-10:50 S100B protein is a new inflammatory suppressor of amyloid-β aggregation | Cláudio Gomes, Portugal

10:50-11:10 SODA: prediction of protein solubility from disorder and aggregation propensity | Silvio Tosatto, Italy


11:10-11:40 - Coffee break


11:40-12:00 Axial co-aggregation of amyloids: from structural principles to in silico prediction | Andrey Kajava, France

12:00-12:20 Phase transition and amyloid formation by a viral protein as an additional molecular mechanism of virus-induced cell toxicity | Sonia Longhi, France

12:20-12:40 hnRNPDL isoforms possess distinct assembly properties and disease-causing mutations increase their aggregation propensity | Cristina Batlle, Spain


12:40-14:00 Lunch






14:00-14:20 High throughput screening combined with computational modeling identify novel small molecules as modulators of Tau aggregation in vitro and in Alzheimer's animal model | Daniel Segal, Israel

14:20-14:50 Molecular-tweezer inhibitors of Tau aggregation and tauopathy | Gal Bitan, USA

14:50-15:10 Inhibition of SOD1 protein self-assembly in vitro and in the transgenic G93A-SOD1 mouse model of Amyotrophic Lateral Sclerosis by the molecular tweezer CLR01 | Martina Wiedau, USA


15:10-16:30 Coffee break & Poster Session




16:30-17:00 Seeing amyloid and its assembly mechanisms | Sheena Radford, UK

17:00-17:30 Lysosomal storage diseases as a new class of amyloidosis | Alessandro Fraldi, Italy

17:30-17:50 Small molecules as modulators of TTR aggregation | Maria Rosário Almeida, Portugal

17:50-18:10 Using luciferase mutants to study the impact of serotonergic signaling modulation of proteostasis in C. elegans | Bruna Lomba, Portugal




22nd March 2019




9:00-9:30 Targeting alpha-synuclein pathology in cellular and animal models of Parkinson’s | Richard Wade-Martins, UK

9:30-9:50 A novel small molecule inhibits α-synuclein aggregation, disrupts amyloid fibrils and prevents degeneration of dopaminergic neurons | Salvador Ventura, Spain

9:50-10:10 Molecular tweezer protects against alpha-synuclein-induced neuronal toxicity | E. Faggiani, France

10:10-10:40 Anti-amyloid and antiviral activity of molecular tweezers | Jan Münch, Germany


10:40-12:00 Coffee break & Poster Session


12:00-13:00 Plenary Talk:

Supramolecular aggregation inhibitors | Thomas Schrader, Germany


13:00-14:30 Lunch




14:30-15:00 Modulating ataxin-3 self-assembly pathway | Sandra Ribeiro, Portugal

15:00-15:30 Conformational polymorphisms of amyloid Aß and implications for immunotherapeutic development | Charles Glabe, USA

15:30-15:50 Untangling the conformational plasticity of Tau through single-molecule FRET | Ana Melo, Portugal

15:50-16:10 Solution NMR Studies of APPTM | Chunyu Wang, USA


16:10 Final Remarks



Confirmed speakers


Maria Rosário Almeida, Ph.D. - i3S/ IBMC, ICBAS, University of Porto, Portugal

Gal Bitan, Ph.D. – UCLA

Fabrizio Chiti, Ph.D. - University of Florence, Italy

Alessandro Fraldi, Ph.D. - University of Naples "Federico II", Italy

Jan Münch, Ph.D. - Ulm University, Germany

Sheena Radford, Ph.D. - University of Leeds, United Kingdom

Sandra de Macedo Ribeiro, Ph.D. - i3S/ IBMC, University of Porto, Portugal

Thomas Schrader, Ph.D. - University of Duisburg-Essen, Germany

Richard Wade-Martins, MA, DPhil - Oxford University, United Kingdom




Organizing Committee


Sandra de Macedo Ribeiro, i3S/ IBMC, University of Porto
Maria Rosário Almeida, i3S/ IBMC, ICBAS, University of Porto
Gal Bitan, UCLA

Abstract Submission

The deadline for abstract submission is 10th February 2019


Authors should follow the abstract layout template provided:




Abstracts will be reviewed by the organizing committee and a decision whether to accept the abstract will be sent by 15th February 2019.

During abstract submission, authors are asked to indicate whether they have a preference for oral or poster presentation






Registration fee includes coffee breaks, lunch (on 22nd March) and workshop material.







Early bird registration | Until 31st January 2019 (Payment deadline: 7th February 2019)

Regular registration: 65 €

Students and Postdocs (up to 5 years after Ph.D.)*: 35 €


Late registration |  From 1st February until 28th February 2019 (Payment deadline: 7th March 2019)

Regular registration: 100 €

Students and Postdocs (up to 5 years after Ph.D.)*: 50 €


*Students and Postdocs (up to 5 years after Ph.D.) should enclose a document confirming their status in the registration form.






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