Interaction of decorin with CNBr peptides from collagens I and II. Evidence for multiple binding sites and essential lysyl residues in collagen.

摘要: Decorin is a small leucine-rich chondroitin/dermatan sulfate proteoglycan reported to interact with fibrillar collagens through its protein core and localize at d e bands of the collagen fibril banding pattern. Using solid-phase assay, we have determined interaction peptides derived by CNBr cleavage type I II decorin extracted from bovine tendon recombinant preparation. At least five been found all three samples. The has dissociation constant in nanomolar range. triple helical conformation peptide trimeric species necessary requisite for binding. All positive region within fibrils. Two chemical derivatives were prepared N-acetylation N-methylation primary amino group Lys/Hyl side chains. Chemical modifications performed mild conditions do not significantly alter thermal stability whereas they affect decorin: eliminates both charge binding decorin, preserves cationic character modulates We conclude that makes contacts multiple sites probably also some residues are essential