TAILIEUCHUNG - Báo cáo Y học: Interaction of decorin with CNBr peptides from collagens I and II Evidence for multiple binding sites and essential lysyl residues in collagen

Decorin is a small leucine-rich chondroitin/dermatan sulfate proteoglycan reported to interact with ®brillar collagens through its protein core and to localize atdandebands of the collagen ®bril banding pattern. Using a solid-phase assay, we have determined the interaction of peptides derivedbyCNBr cleavage of type I and type II collagenwith decorin extracted from bovine tendon and its protein core and with a recombinant decorin preparation. | Eur. J. Biochem. 269 1428-1437 2002 FEBS 2002 Interaction of decorin with CNBr peptides from collagens I and II Evidence for multiple binding sites and essential lysyl residues in collagen Ruggero Tenni1 I Manuela Viola1 Franz Welser2 Patrizia Sini1 Camilla Giudici1 Antonio Rossi1 and M. Enrica Tira1 1 Dipartimento di Biochimica A. Castellani University of Pavia Italy 2EMP Genetech Denzlingen Germany 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-acetyla-tion 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. Keywords collagen decorin collagen peptides proteoglycans protein-protein .

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