AUGUST 24 – 27, 2009 – Copenhagen, Denmark
Organizing committee: Daniel Otzen (Aarhus), Poul Henning Jensen (Aarhus), Sven Frøkjær (Copenhagen) & Niels Borregaard (Copenhagen) Invited speakers and chairmen: BERTOLOTTI, Anne (United Kingdom) – BRANDT, Roland (Germany) – CHAPMAN, Matthew R. (USA) – EISENBERG, David (USA) – GEBBINK, Martijn (The Netherlands) – HARTL, F. Ulrich (Germany) – JENSEN, Poul Henning (Denmark) – KELLY, Jeffery (USA) – KNOWLES, Tuomas (United Kingdom) – KOPITO, Ron (USA) – LANSBURY, Peter (USA) – MASLIAH, Eliezer (USA) – MASTERS, Colin L. (Australia) – MORIMOTO, Richard I. (USA) – NIELSEN, Per Halkjær (Denmark) – OTZEN, Daniel (Denmark) – OUTEIRO, Tiago F. (Portugal) – REINHART, Peter (USA) – SARAIVA, Maria João (Portugal) – SCHEIBEL, Thomas (Germany) – SERPELL, Louise (United Kingdom) – VENDRUSCOLO, Michele (United Kingdom) – VESTERGAARD, Bente (Denmark) – WALSH, Dominic M. (Ireland) – WANKER, Erich E. (Germany) – ZHANG, Shuguang (USA)
Synopsis: Proteins play a central role for all organisms by virtue of a well-defined three-dimensional structure, obtained through a complex but well-regulated folding process. Folding can be compromised by proteolysis, mutagenesis or chemical changes within the cell. If the misfolded protein is not cleared sufficiently rapidly by the cellular control system, aggregates in various guises may accumulate in the cell. Early stage aggregation species include cytotoxic oligomers thought to permeabilize cell membranes and inhibit the protein degradation machinery. Such oligomers are increasingly implicated in prevalent diseases such as Parkinson’s and Alzheimer’s. The mature fibrils formed at later stages are apparently mainly a problem in systemic amyloidoses where they accumulate in vital organs to an extent that leads to organ failure. There is intense research in therapeutic strategies, including vaccination against early-stage aggregates.
Recent discoveries highlight the functional role of protein amyloid within human melanosomes, bacterial biofilm and other areas, and there is increasing awareness of the nanotechnological potential of such highly organized structures. The Benzon Symposia are international conferences on front line research in medical, pharmaceutical, and related sciences funded by the Alfred Benzon Foundation.
The 56th Benzon Symposium on Functional and Pathogenic Protein Aggregation will provide a very comprehensive approach to the subject of protein fibrillation. Topics include amyloid and oligomer structures, mechanisms of formation in vitro and in vivo, pathological consequences, therapeutic approaches and functional applications in vitro and in vivo. In particular we will address the following questions: What is the link between aggregate-membrane interactions and pathological mechanisms? Which alternative mechanisms can explain the pathological observations and how can experiments be designed to clarify the molecular mechanisms? How can we develop molecular strategies against deposition diseases? Functional amyloid is the result of a very long evolutionary optimization in contrast to pathological amyloid. Can the two phenomena be distinguished based on their fundamental biophysical properties or is it a question of cellular regulation?
There is growing evidence for fibrillar polymorphism, i.e. the ability of a protein to adopt different aggregate structures with different structures and stabilities. Can these properties be systematized and modelled in silico? What, if any, is their physiological significance? Fibrillation is a striking example of a well-developed ability to self-organize. Can these properties be tuned in tailor-made fashion towards pharmaceutical and nanotechnological solutions?
Scientific program (pdf)