Authors: Duus, K.; Sandhu, N.; Jorgensen, C. S.; Hansen, P. R.; Steino, A.; Thaysen-Andersen, M.; Hojrup, P.; Houen, G.

Source: Protein and Peptide Letters, Volume 16, Number 11, November 2009 , pp. 1414-1423(10)

Publisher: Bentham Science Publishers

Abstract:

The interaction of calreticulin with native and denatured forms and polypeptides in proteolytic digests of proteins representing structural classes of all-α-helix (hemoglobin, serum albumin), all-β-sheet (IgG) and α-helix + β-sheets (lysozyme, ovalbumin) was investigated. The binding of calreticulin to denatured proteins was found to depend on conformation and structural class of the protein. No interaction was observed with the native proteins, whereas binding was seen for the denatured proteins, the order of interaction being lysozyme = IgG > ovalbumin ≫ hemoglobin = serum albumin. Moreover, the interaction between calreticulin and the heat-denatured proteins depended on the temperature and time used for denaturation and the degree of proteolytic fragmentation. Calreticulin bound well to peptides in proteolytic digests from protease K or chymotrypsin treatment of lysozyme, IgG and ovalbumin but weakly or not at all to peptides in proteolytic digests of hemoglobin and serum albumin. Synthetic peptides from lysozyme and ovalbumin confirmed binding to hydrophobic peptides from these proteins. These results show that calreticulin has the ability to interact with denatured and fragmented forms of proteins with a preference for β-strand structure and hydrophobicity.

Keywords: Calreticulin; peptide specificity; chaperone; structural class; α-helix; β-sheet

Document Type: Research article

DOI: http://dx.doi.org/10.2174/092986609789353772

Publication date: 2009-11-01

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• Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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