Abstract
In the presence of ginkgolides A and B a recombinant human prion protein (90-231) is more susceptible to proteolysis, which is characteristic for the non-infective form of prion proteins and more thermostable than in the absence of ginkgolides. Probably, ginkgolides exert a neuroprotective effect through a rearrangement of the prion structure.
Keywords: Three-dimensional structure, structural transformation, ginkgolide, prion protein, protein misfolding
Protein & Peptide Letters
Title: Interactions of Ginkgolides A and B with a Recombinant Human Prion Protein
Volume: 17 Issue: 3
Author(s): Dessislava Georgieva, Lars Redecke, Martin von Bergen, Nicolay Genov and Chrsitian Betzel
Affiliation:
Keywords: Three-dimensional structure, structural transformation, ginkgolide, prion protein, protein misfolding
Abstract: In the presence of ginkgolides A and B a recombinant human prion protein (90-231) is more susceptible to proteolysis, which is characteristic for the non-infective form of prion proteins and more thermostable than in the absence of ginkgolides. Probably, ginkgolides exert a neuroprotective effect through a rearrangement of the prion structure.
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Cite this article as:
Georgieva Dessislava, Redecke Lars, Bergen von Martin, Genov Nicolay and Betzel Chrsitian, Interactions of Ginkgolides A and B with a Recombinant Human Prion Protein, Protein & Peptide Letters 2010; 17 (3) . https://dx.doi.org/10.2174/092986610790780314
DOI https://dx.doi.org/10.2174/092986610790780314 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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