Welcome

Numerous proteins and peptides have the capacity to self-assemble into amyloid fibrils. Very little is known about the function of amyloids. The molecular basis for toxicity of amyloids is poorly understood. The presence of functional amyloids reinforces the emerging concept of the amyloid fold as a quaternary protein structure that is able to carry out a diversity of biological functions and that is subject to regulation, avoiding toxicity. Amyloid dynamics appear more dynamic than previously anticipated and this challenges the dogma that amyloid fibrils are end-stage structures.

In this Advanced Course we have brought together a unique combination of frontiers in science in the field of protein folding, aggregation and compartmentalization who will meet with young researchers already active in -or considering entering- this research field and who will discuss their mutual results. A special focus will be on technological advances for developing novel research strategies and to interfere with protein folding and amyloid formation for drug development.

In the special evening lectures, frontiers in science will discuss the different topics in an integrative manner, providing a clear connection between the different sessions. The course will be organized in an informal setting to facilitate contacts and information exchange. Poster sessions, oral presentations, round table discussions and informal meet-the-expert sessions are scheduled to stimulate interactions between the participants and the lecturers/tutors.

We look forward to welcoming you on the Island of Spetses!

The Organizers

Deadlines

  • Applications Opening
    Jan 1, 2021
  • Youth Travel Fund Grants (closing)
    May 14, 2021
  • Applications closing
    June 1, 2021

FEBS has twin commitments to high-quality publications and the promotion of molecular biosciences. As a charitable academic organization,
FEBS uses income from the journals to fund its diverse activities, including support for FEBS Advanced Courses.