Peptide binding specificity of the chaperone calreticulin

Noreen Sandhu, Karen Duus, Charlotte S Jørgensen, Paul R Hansen, Susanne W Bruun, Lars Ø Pedersen, Peter Højrup, Gunnar Houen

Research output: Contribution to journalJournal articleResearchpeer-review


Calreticulin is a molecular chaperone with specificity for polypeptides and N-linked monoglucosylated glycans. In order to determine the specificity of polypeptide binding, the interaction of calreticulin with polypeptides was investigated using synthetic peptides of different length and composition. A large set of available synthetic peptides (n=127) was tested for binding to calreticulin and the results analysed by multivariate data analysis. The parameter that correlated best with binding was hydrophobicity while beta-turn potential disfavoured binding. Only hydrophobic peptides longer than 5 amino acids showed binding and a clear correlation with hydrophobicity was demonstrated for oligomers of different hydrophobic amino acids. Insertion of hydrophilic amino acids in a hydrophobic sequence diminished or abolished binding. In conclusion our results show that calreticulin has a peptide-binding specificity for hydrophobic sequences and delineate the fine specificity of calreticulin for hydrophobic amino acid residues.
Original languageEnglish
JournalBBA General Subjects
Issue number6
Pages (from-to)701-713
Number of pages12
Publication statusPublished - 1. Jun 2007



  • Amino Acid Sequence
  • Amino Acids
  • Calreticulin
  • Histocompatibility Antigens Class I
  • Humans
  • Hydrophobicity
  • Molecular Chaperones
  • Molecular Sequence Data
  • Peptide Fragments
  • Prions
  • Protein Binding
  • Sensitivity and Specificity
  • Serum Amyloid P-Component

Cite this

Sandhu, N., Duus, K., Jørgensen, C. S., Hansen, P. R., Bruun, S. W., Pedersen, L. Ø., Højrup, P., & Houen, G. (2007). Peptide binding specificity of the chaperone calreticulin. BBA General Subjects, 1774(6), 701-713.