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Mini Review

Design and syntheses of peptides which induce or enhance structural changes of recombinant bovine prion protein (rbPrP) and discovery of peptides from bovine brain which accelerate structural conversions of rbPrP

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Pages 117-118 | Received 18 Nov 2013, Accepted 22 Jan 2014, Published online: 07 Feb 2014

Figures & data

Figure 1. Prion related synthetic peptide fragments and the de novo designed peptide for the structural conversion, designated HPPSH. Each Cys-residue was replaced by a Ser-residue to avoid disulfide bond formation. Hence hPrP170–175 (SNQNNF) formed parallel β-sheet [PDB ID: 2OL9] and hPrP180–195 (VNITIKQHTVTTTTKG) formed α-helix [PDB ID: 2IV4].

Figure 1. Prion related synthetic peptide fragments and the de novo designed peptide for the structural conversion, designated HPPSH. Each Cys-residue was replaced by a Ser-residue to avoid disulfide bond formation. Hence hPrP170–175 (SNQNNF) formed parallel β-sheet [PDB ID: 2OL9] and hPrP180–195 (VNITIKQHTVTTTTKG) formed α-helix [PDB ID: 2IV4].

Figure 2. Scheme for the preparation of peptide library derived bovine brain. Abbreviations used are CF, centrifugation (10 000 rpm, 4 °C); PPT, precipitate; SCA, structural conversion assay. Chromatogram is a tryptic digests and fractions eluted at 7–8 and 15–16 min (arrow) exhibited significance in SCA.

Figure 2. Scheme for the preparation of peptide library derived bovine brain. Abbreviations used are CF, centrifugation (10 000 rpm, 4 °C); PPT, precipitate; SCA, structural conversion assay. Chromatogram is a tryptic digests and fractions eluted at 7–8 and 15–16 min (arrow) exhibited significance in SCA.

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