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Current Topics in Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 1568-0266
ISSN (Online): 1873-4294

Computational Studies on the Prion Protein

Author(s): Giulia Rossetti, Salvatore Bongarzone and Paolo Carloni

Volume 13 , Issue 19 , 2013

Page: [2419 - 2431] Pages: 13

DOI: 10.2174/15680266113136660170

Price: $65

Abstract

Prion diseases are rare neurodegenerative diseases characterized by the conversion of the prion protein from its native state (PrPC) towards the so-called 'scrapie form', rich in β-strands. Computational approaches, here briefly reviewed, are instrumental to understand the intrinsic instability of PrPC fold and how the latter is affected by mutations, binding of metals as well as by different environmental conditions, such as pH and temperature. These studies also provide a structural basis for the binding of anti-prion compounds, which may block the conversion to the scrapie form and, consequently, may inhibit fibril formation.

Keywords: Prion proteins, native state, scrapie form, molecular simulation, bioinformatics, molecular docking.


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