High Pressure Tuning of Biochemical Processes: Protein dynamics and aggregation

Laszlo Smeller 

Semmelweis University of Medicine, Institute of Biophysics and Radiation Biology, Budapest, Hungary


Since deposition of insoluble protein aggregates can be found in many serious diseases like Alzheimer’s disease, familial amyloidosis, investigation of protein aggregation is a very important research topic. Pressure sensitivity of the protein aggregation makes high pressure a useful tool in these experiments.

The 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.

The volumetric aspects of protein interacitions were also investigated with number of spectroscopical and other methods from infrared and fluorescence spectroscopy, to pressure perturbation calorimetry.



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Related papers
  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

Presentation: Invited at COST D30 Final Evaluation Meeting, by Laszlo Smeller
See On-line Journal of COST D30 Final Evaluation Meeting

Submitted: 2007-10-20 15:37
Revised:   2009-06-07 00:44