Coating of Titanium Implant Materials with Thin Polymeric Films for Binding the Signaling Protein BMP2

Lorenz, Corinna; Hoffmann, Andrea; Groß, Gerhard; Windhagen, H.; Dellinger, Philip; Möhwald, Kai; Dempwolf, Wibke; Menzel, Henning

doi:10.1002/mabi.201000342

Cited by 22 publications

(11 citation statements)

References 52 publications

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“…BMP Responsive Element Luciferase (BRE-Luc) assay. The assay was conducted essentially as described previously [35] with the following modifications. To generate a stable reporter cell line, the mouse muscle satellite cell line C2C12 was transfected with the BREfirefly luciferase reporter plasmid containing an inhibitor of the differentiation promotorluciferase construct from Korchinsky et al [36].…”

Section: Bioactivity Measurementsmentioning

confidence: 99%

Properties of dimeric, disulfide-linked rhBMP-2 recovered from E. coli derived inclusion bodies by mild extraction or chaotropic solubilization and subsequent refolding

Quaas¹,

Burmeister

Li³

et al. 2018

Process Biochemistry

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Recombinant human bone morphogenetic protein-2 (rhBMP-2), a cystine-knot containing disulfide linked homodimer, was produced in form of inclusion bodies (IBs) using E. coli BL21 (DE3) and SHuffle T7 Express. Non-reducing SDS-PAGE analysis revealed that rhBMP-2 was present within IBs in both strains as monomer and in form of disulfide-linked dimers. Purified dimeric disulfide-linked rhBMP-2 was obtained from IBs by two different methods. The first method involved classical solubilisation using strong denaturants and subsequent refolding. The second method involved mild extraction without refolding. Both rhBMP-2 dimer variants were purified by Heparin-affinity chromatography. Mildly extracted rhBMP-2 was further purified by size-exclusion chromatography. The resulting dimeric rhBMP-2 variants were studied regarding bioactivity and folding status. In contrast to the rhBMP-2 dimer obtained by classical refolding it was shown that the disulfide-linked dimer obtained by mild extraction was not correctly folded e.g. the hydrophobic core not correctly formed. Moreover, refolded dimeric rhBMP-2 was bioactive and the mildly extracted dimeric rhBMP-2 did not show any bioactivity. Disulfide-bond analysis revealed that the intricate disulfide-bond pattern of the complex cystine-knot scaffold was not present in the IB embedded disulfide-linked rhBMP-2 dimer but was formed later during classical refolding of the reduced protein under appropriate redox conditions.

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Section: Bioactivity Measurementsmentioning

confidence: 99%

Properties of dimeric, disulfide-linked rhBMP-2 recovered from E. coli derived inclusion bodies by mild extraction or chaotropic solubilization and subsequent refolding

Quaas¹,

Burmeister

Li³

et al. 2018

Process Biochemistry

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“…In these studies, only a fraction of the tethered rhBMP-2 was accessible to cells because it was tethered inside the polymer network. The accessibility of rhBMP-2 in this system could be improved by including PEG spacer molecules in the polymer to give cells better access to the growth factor (204). These approaches present the broad-based utility of covalently tethering rhBMP-2 to biomaterials through surface exposed primary amines and carboxylic acids.…”

Section: Future Directionsmentioning

confidence: 99%

Growth factor delivery: How surface interactions modulate release in vitro and in vivo

King

Krebsbach

2012

Advanced Drug Delivery Reviews

174

134

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Biomaterial scaffolds have been extensively used to deliver growth factors to induce new bone formation. The pharmacokinetics of growth factor delivery has been a critical regulator of their clinical success. This review will focus on the surface interactions that control the non-covalent incorporation of growth factors into scaffolds and the mechanisms that control growth factor release from clinically relevant biomaterials. We will focus on the delivery of recombinant human bone morphogenetic protein-2 from materials currently used in the clinical practice, but also suggest how general mechanisms that control growth factor incorporation and release delineated with this growth factor could extend to other systems. A better understanding of the changing mechanisms that control growth factor release during the different stages of preclinical development could instruct the development of future scaffolds for currently untreatable injuries and diseases.

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“…On the other hand, in order to create stable covalent immobilization, Puleo et al [21] performed plasma polymerization of allylamine on a titanium surface. Meanwhile, others prepared chitosan, dextran, or polymer layers on titanium to covalently immobilize BMP [22–25]. …”

Section: Introductionmentioning

confidence: 99%

Immobilization of Bone Morphogenetic Protein on DOPA- or Dopamine-Treated Titanium Surfaces to Enhance Osseointegration

Kang

Tada

Kitajima

et al. 2013

BioMed Research International

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Titanium was treated with 3,4-dihydroxy-L-phenylalanine (DOPA) or dopamine to immobilize bone morphogenetic protein-2 (BMP2), a biomolecule. DOPA and dopamine solutions turned into suspensions, and precipitates were produced at high pH. Both treatments produced a brown surface on titanium that was thicker at high pH than low pH. Dopamine produced a thicker layer than DOPA. The hydrophobicity of the surfaces increased after treatment with dopamine independent of pH. Furthermore, there were more amino groups in the layers formed at pH 8.5 than pH 4.5 in both treatments. Dopamine treatment produced more amino groups in the layer than DOPA. BMP2 was immobilized on the treated surfaces via a coupling reaction using carbodiimide. More BMP2 was immobilized on surfaces treated at pH 8.5 than pH 4.5 in both treatments. The immobilized BMP induced specific signal transduction and alkali phosphatase, a differentiation marker. Thus, the present study demonstrates that titanium treated with DOPA or dopamine can become bioactive via the surface immobilization of BMP2, which induces specific signal transduction.

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Coating of Titanium Implant Materials with Thin Polymeric Films for Binding the Signaling Protein BMP2

Cited by 22 publications

References 52 publications

Properties of dimeric, disulfide-linked rhBMP-2 recovered from E. coli derived inclusion bodies by mild extraction or chaotropic solubilization and subsequent refolding

Properties of dimeric, disulfide-linked rhBMP-2 recovered from E. coli derived inclusion bodies by mild extraction or chaotropic solubilization and subsequent refolding

Growth factor delivery: How surface interactions modulate release in vitro and in vivo

Immobilization of Bone Morphogenetic Protein on DOPA- or Dopamine-Treated Titanium Surfaces to Enhance Osseointegration

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