Modifications of hyaluronan influence the interaction with human bone morphogenetic protein-4 (hBMP-4).
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 microM. 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.
Hintze
Vera
V
Institute of Material Science, Max Bergmann Center of Biomaterials, Technische Universität Dresden, 01069 Dresden, Germany. Vera.Hintze@tu-dresden.de
Moeller
Stephanie
S
Schnabelrauch
Matthias
M
Bierbaum
Susanne
S
Viola
Manuela
M
Worch
Hartmut
H
Scharnweber
Dieter
D
D015374:Biosensing Techniques; D055415:Bone Morphogenetic Protein 4 / Q000737:chemistry* / Q000235:genetics; D002809:Chondroitin Sulfates / Q000737:chemistry; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D006820:Hyaluronic Acid / Q000737:chemistry*; D055767:Immobilized Proteins / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D013463:Sulfuric Acid Esters / Q000737:chemistry*; D020349:Surface Plasmon Resonance
C525809:BMP4 protein, human; D055415:Bone Morphogenetic Protein 4; D055767:Immobilized Proteins; D011994:Recombinant Proteins; D013463:Sulfuric Acid Esters; D006820:Hyaluronic Acid; D002809:Chondroitin Sulfates