Protein aggregation is a very important research topic, since deposition of insoluble protein aggregates can be found in many serious diseases like Alzheimer's disease, familial amyloidosis.

This presentation summarizes the achievements of the COST D30 WG006.

The high pressure - temperature phase diagram of the proteins was extended, to incorporate the intermediate and aggregated protein phases.

The physicochemical aspects of the polymorphism of amyloids, as well as the role of hydrational and volumetric factors in amyloidogenesis were also studied. As a result a physicochemical, solvational model explaining how preferential hydration or preferential binding of a cosolvent to an amyloidgenic protein may lead to different "strains" has been put forward.

The stability of amyloid fibrils towards high hydrostatic pressure was studied and found markedly different from the stability of the amorpous aggregates.

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1. High Pressure Tuning of Biochemical Processes: Protein dynamics and aggregation
2. Pressure-Assisted Cold Denaturation of Proteins Compared to Pressure and Heat Denaturation. Application to Food Components
3. Temperature-Pressure Phase Diagrams of Proteins
4. Intermolecular Interactions of Proteins under Pressure. Aggregation, Dissociation, Chaperoning