| Title | Application of the atomic force microscopy technique to the study of recombinant prion protein and its potential ligand interactions | |
| Author | G. Bloukas1, K. Kotta1, S. Kunze2, S. Gnoth2, J. Metze2, W. Bodemer3, C.H. Panagiotidis1 and T. Sklaviadis1
1Group of Transmissible Spongiform Encephalopathies, Laboratory of Pharmacology, Pharmaceutical Department, Aristotle University of Thessaloniki, 541 24, Greece. 2Ιnstitute for Bioprocessing and Analytical Measurement Techniques e.V., Rosenhof, D-37308 Heilbad Heiligenstadt, Germany. 3German Primate Center, Kelfnerweg 4, D- 37077 Gottingen, Germany |
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| Citation | Bloukas, G., Kotta, K., Kunze, S., Gnoth, S., Metze, J., et al.: Application of the atomic force microscopy technique to the study of recombinant prion protein and its potential ligand interactions, Epitheorese Klin. Farmakol. Farmakokinet. 18(1): 45-48 (2004) | |
| Publication Date | Accepted for publication: 2004 | |
| Full Text Language | English | |
| Order – Buy | Ηλεκτρονική Μορφή: pdf (10 €) – Digital Type: pdf (10 €) pharmakonpress[at]pharmakonpress[.]gr | |
| Keywords | Atomic Force Microscopy, PrP | |
| Other Terms | review article | |
| Summary | The technique of Atomic Force Microscopy is a novel method for the direct observation of biomolecules and their surface topography. The technique has been used since the beginning of 1980 and it contributes to the analysis of single proteins and protein assemblies. It can also monitor conformational changes directly under native conditions. Therefore it is considered appropriate for the investigation of direct interaction forces between PrP molecules or between PrP and their suspected ligands, such as peptides and antibodies. Moreover, the technique is unique, since the results of such an investigation can lead to the clarification of factors that favour or inhibit the transition of the normal prion protein to its pathological isoform. In the long run it may even lead to the development of therapeutic schemes to treat prion diseases. | |
| References | 1. Engel A.t Muller D.J.: Observing single biomolecules at work with the atomic force microscope. Nature Struct. Biol. 7: 715-718 (2000)
2. Levy Y., Becker O.M.: Conformational polymorphism of wild type and mutant prion proteins: Energy landscape analysis. Proteins 47: 458-468 (2002) 3. Rief M., Grubmuller H: Force spectroscopy of single biomolecules. Chem. Phys. Chem. 3: 255-261 (2002) 4. Quin K.F., Yang Y., Chishti M.A., ‘Meng L.J., Kretzsch- mar H.A., Yip C.M., Fraser P.E., Westàway D.: Copper (II)- induced conformational changes and protease resistance in recombinant and cellular PrP, Effect of protein age and deamidation. J. Biol. Chem. 275: 19121-19131 (2000) 5. Engel A., Lyubchenko Y., Muller D.: Atomic Force Microscopy: a powerful tool to observe biomolecules at work. Trends Cell Biol. 9. 77-80 (1999) |
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| Relative Papers |
Online ISSN 1011-6575
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Articles published in this Journal are Indexed or Abstracted in: • Chemical Abstracts • Elsevier’s Bibliographic Databases: Scopus, EMBASE, EMBiology, Elsevier BIOBASE SCImago Journal and Country Rank Factor
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| ΕΤΗΣΙΑ ΣΥΝΔΡΟΜΗ 2004 – ANNUAL SUBSCRIPTION 2004 | |
| Γλώσσα Πλήρους Κειμένου – Full Text Language | Αγγλικά – English |
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