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Modifications of Hyaluronan Influence the Interaction with Human Bone Morphogenetic Protein-4 (hBMP-4)

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Vera Hintze*^†, Stephanie Moeller^‡, Matthias Schnabelrauch^‡, Susanne Bierbaum^†, Manuela Viola^§, Hartmut Worch^† and Dieter Scharnweber^†

Institute of Material Science, Max Bergmann Center of Biomaterials, Technische Universität Dresden, 01069 Dresden, Germany, Biomaterials Department, INNOVENT e.V., 07745 Jena, Germany, and Department of Experimental and Clinical Biomedical Sciences, Università dell’Insubria, 21100 Varese, Italy

Biomacromolecules, 2009, 10 (12), pp 3290–3297

DOI: 10.1021/bm9008827

Publication Date (Web): November 6, 2009

* To whom correspondence should be addressed. E-mail: Vera.Hintze@tu-dresden.de., †

Technische Universität Dresden.

, ‡

INNOVENT e.V.

, §

Università dell’Insubria.

Section:

Pharmaceuticals

Abstract

In this study, we have demonstrated that the modification of hyaluronan (hyaluronic acid; Hya) with sulfate groups led to different binding affinities for recombinant human bone morphogenetic protein-4 (rhBMP-4). The high-sulfated sHya2.8 (average degree of sulfation (D.S.) 2.8) exhibited the tightest interaction with rhBMP-4, followed by the low-sulfated sHya1.0, as determined with surface plasmon resonance (SPR), ELISA, and competition ELISA. Unmodified Hya, chondroitin-sulfate (CS), and heparan sulfate (HS) showed significantly less binding affinity. SPR data could be fitted to an A + B = AB Langmuir model and binding constants were evaluated ranging from 13 pM to 5.45 μM. The interaction characteristics of the differentially sulfated Hyas are promising for the incorporation of these modified polysaccharides in bioengineered coatings of biomaterials for medical applications.

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