Interactions of ginkgolides A and B with a recombinant human prion protein.
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.
Georgieva
Dessislava
D
Institute of Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King Platz 6, 20146 Hamburg, Germany.
Redecke
Lars
L
von Bergen
Martin
M
Genov
Nicolay
N
Betzel
Chrsitian
C
D046934:Ginkgolides / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D006358:Hot Temperature; D006801:Humans; D008027:Light; D018696:Neuroprotective Agents / Q000378:metabolism; D011328:Prions / Q000737:chemistry* / Q000378:metabolism; D011489:Protein Denaturation / Q000187:drug effects; D017510:Protein Folding; D055550:Protein Stability; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D012542:Scattering, Radiation
D046934:Ginkgolides; D018696:Neuroprotective Agents; D011328:Prions; D011994:Recombinant Proteins