High Pressure Tuning of Biochemical Processes: Protein dynamics and aggregation

Laszlo Smeller 

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

Abstract

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.

 

Legal notice
  • Legal notice:

    Copyright (c) Pielaszek Research, all rights reserved.
    The above materials, including auxiliary resources, are subject to Publisher's copyright and the Author(s) intellectual rights. Without limiting Author(s) rights under respective Copyright Transfer Agreement, no part of the above documents may be reproduced without the express written permission of Pielaszek Research, the Publisher. Express permission from the Author(s) is required to use the above materials for academic purposes, such as lectures or scientific presentations.
    In every case, proper references including Author(s) name(s) and URL of this webpage: http://science24.com/paper/12838 must be provided.

 

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
Google
 
Web science24.com
© 1998-2021 pielaszek research, all rights reserved Powered by the Conference Engine