Note: these authors contributed equally to this work.
Interaction of decorin with CNBr peptides from collagens I and II
Evidence for multiple binding sites and essential lysyl residues in collagen
Article first published online: 1 MAR 2002
European Journal of Biochemistry
Volume 269, Issue 5, pages 1428–1437, March 2002
How to Cite
Tenni, R., Viola, M., Welser, F., Sini, P., Giudici, C., Rossi, A. and Tira, M. E. (2002), Interaction of decorin with CNBr peptides from collagens I and II. European Journal of Biochemistry, 269: 1428–1437. doi: 10.1046/j.1432-1033.2002.02784.x
- Issue published online: 1 MAR 2002
- Article first published online: 1 MAR 2002
- (Received 3 December 2001, accepted 14 January 2002)
- collagen peptides;
- protein–protein interactions
Decorin is a small leucine-rich chondroitin/dermatan sulfate proteoglycan reported to interact with fibrillar collagens through its protein core and to localize at d and e bands of the collagen fibril banding pattern. Using a solid-phase assay, we have determined the interaction of peptides derived by CNBr cleavage of type I and type II collagen with decorin extracted from bovine tendon and its protein core and with a recombinant decorin preparation. At least five peptides have been found to interact with all three decorin samples. The interaction of peptides with tendon decorin has a dissociation constant in the nanomolar range. The triple helical conformation of the peptide trimeric species is a necessary requisite for the binding. All positive peptides have a region within the d and e bands of collagen fibrils. Two chemical derivatives of collagens and of positive peptides were prepared by N-acetylation and N-methylation of the primary amino group of Lys/Hyl side chains. Chemical modifications performed in mild conditions do not significantly alter the thermal stability of peptide trimeric species whereas they affect the interaction with decorin: N-acetylation eliminates both the positive charge and the binding to decorin, whereas N-methylation preserves the cationic character and modulates the binding. We conclude that decorin makes contacts with multiple sites in type I collagen and probably also in type II collagen and that some collagen Lys/Hyl residues are essential for the binding.