A role for His155 in binding of human prion peptide144-167 to immobilised prion protein

J. Richard Hesp*, Neil D.H. Raven, J. Mark Sutton

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


The interactions and conformational changes that lead to the conversion of the normal prion protein (PrPc) to its pathogenic form, PrPsc, are still being elucidated. Using Surface Plasma Resonance (SPR), we provide evidence that a synthetic peptide (PrP144-167) corresponding to residues comprising the α helix 1-β strand 2 domain of PrPc is able to interact and bind to immobilised recombinant human PrP (rHuPrP) in a dose-dependent manner. The interaction is pH dependent with an increase in binding observed as the pH is lowered, particularly between pH 6.5 and pH 5.5 suggesting a specific role for His155 in the interaction, confirmed by covalent modification of this residue in the peptide with diethylpyrocarbonate (DEPC). Circular dichroism analysis of PrP144-167 revealed no secondary structure motifs across the pH range investigated. Possible pH related structural changes of immobilised rHuPrP are also discussed with regard to the increased affinity for PrP144-167.

Original languageEnglish
Pages (from-to)695-699
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 26 Oct 2007

Bibliographical note

Funding Information:
Funding for the study was from the UK Department of Health. The views expressed in the publication are those of the authors and not necessarily those of the Department of Health. The authors gratefully acknowledge Prof. Ravi Acharya and Dr. Laurie Irons, University of Bath, for their expert advice and assistance with the CD analysis.


  • Creutzfeldt-Jakob disease
  • Peptides
  • Prion
  • Surface plasmon resonance
  • Transmissible spongiform encephalopathy


Dive into the research topics of 'A role for His155 in binding of human prion peptide144-167 to immobilised prion protein'. Together they form a unique fingerprint.

Cite this