Oligomeric forms of peptide fragment PrP(214-226) in solution are preferentially recognized by PrP super(S) super(c)-specific antibody

Oligomeric forms of peptide fragment PrP(214-226) in solution are preferentially recognized by PrP super(S) super(c)-specific antibody

A specific monoclonal antibody (mAb) V5B2 that discriminates between brain tissue of Creutzfeldt-Jakob disease patients and that from normal controls without proteinase K digestion has been prepared using a 13-residue synthetic peptide P1 from the primary structure of human PrP. In the light of the...

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Veröffentlicht in:Biochemical and biophysical research communications 2006-06, Vol.344 (4), p.1320-1326
Hauptverfasser: Ulrih, N P, Skrt, M, Veranic, P, Galvani, V, Vranac, T, Serbec, V C
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container_issue 4
container_start_page 1320
container_title Biochemical and biophysical research communications
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creator Ulrih, N P
Skrt, M
Veranic, P
Galvani, V
Vranac, T
Serbec, V C
description A specific monoclonal antibody (mAb) V5B2 that discriminates between brain tissue of Creutzfeldt-Jakob disease patients and that from normal controls without proteinase K digestion has been prepared using a 13-residue synthetic peptide P1 from the primary structure of human PrP. In the light of the specific interaction between mAb V5B2 and the pathological isoform of PrP (PrP super(S) super(c)), we investigated the solution behavior of antigen P1 and its interactions with mAb V5B2. Our results show that V5B2 recognizes epitope P1 in dimeric/oligomeric forms in solution and in the fibril-like aggregates, as well as in PrP super(S) super(c) aggregates, and demonstrate that the specific epitope is present in all of these forms, but not in PrP super(C).
doi_str_mv 10.1016/j.bbrc.2006.04.046
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title Oligomeric forms of peptide fragment PrP(214-226) in solution are preferentially recognized by PrP super(S) super(c)-specific antibody
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