Sustained delivery of recombinant human bone morphogenetic protein-2 from perlecan domain I - functionalized electrospun poly (ε-caprolactone) scaffolds for bone regeneration

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dc.citation.articleNumber25en_US
dc.citation.journalTitleJournal of Experimental Orthopaedicsen_US
dc.citation.volumeNumber3en_US
dc.contributor.authorChiu, Yu-Chiehen_US
dc.contributor.authorFong, Eliza L.S.en_US
dc.contributor.authorGrindel, Brian J.en_US
dc.contributor.authorKasper, Fred K.en_US
dc.contributor.authorHarrington, Daniel Antonen_US
dc.contributor.authorFarach-Carson, Mary C.en_US
dc.contributor.orgBioengineeringen_US
dc.contributor.orgBiosciencesen_US
dc.date.accessioned2016-11-22T15:16:07Zen_US
dc.date.available2016-11-22T15:16:07Zen_US
dc.date.issued2016en_US
dc.description.abstractBackground: Biomaterial scaffolds that deliver growth factors such as recombinant human bone morphogenetic proteins-2 (rhBMP-2) have improved clinical bone tissue engineering by enhancing bone tissue regeneration. This approach could be further improved if the controlled delivery of bioactive rhBMP-2 were sustained throughout the duration of osteogenesis from fibrous scaffolds that provide control over dose and bioactivity of rhBMP-2. In nature, heparan sulfate attached to core proteoglycans serves as the co-receptor that delivers growth factors to support tissue morphogenesis. Methods: To mimic this behavior, we conjugated heparan sulfate decorated recombinant domain I of perlecan/HSPG2 onto an electrospun poly(ε-caprolactone) (PCL) scaffold, hypothesizing that the heparan sulfate chains will enhance rhBMP-2 loading onto the scaffold and preserve delivered rhBMP-2 bioactivity. Results: In this study, we demonstrated that covalently conjugated perlecan domain I increased loading capacity of rhBMP-2 onto PCL scaffolds when compared to control unconjugated scaffolds. Additionally, rhBMP-2 released from the modified scaffolds enhanced alkaline phosphatase activity in W20–17 mouse bone marrow stromal cells, indicating the preservation of rhBMP-2 bioactivity indicative of osteogenesis. Conclusions: We conclude that this platform provides a sophisticated and efficient approach to deliver bioactive rhBMP-2 for bone tissue regeneration applications.en_US
dc.identifier.citationChiu, Yu-Chieh, Fong, Eliza L.S., Grindel, Brian J., et al.. "Sustained delivery of recombinant human bone morphogenetic protein-2 from perlecan domain I - functionalized electrospun poly (ε-caprolactone) scaffolds for bone regeneration." <i>Journal of Experimental Orthopaedics,</i> 3, (2016) Springer: http://dx.doi.org/10.1186/s40634-016-0057-1.en_US
dc.identifier.doihttp://dx.doi.org/10.1186/s40634-016-0057-1en_US
dc.identifier.urihttps://hdl.handle.net/1911/92715en_US
dc.language.isoengen_US
dc.publisherSpringeren_US
dc.rightsThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License, which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en_US
dc.subject.keywordHeparan sulfateen_US
dc.subject.keywordPoly(ε-caprolactone)en_US
dc.subject.keywordbone morphogenetic proteinen_US
dc.subject.keywordalkaline phosphataseen_US
dc.subject.keywordPerlecan/HSPG2en_US
dc.subject.keywordbone regenerationen_US
dc.titleSustained delivery of recombinant human bone morphogenetic protein-2 from perlecan domain I - functionalized electrospun poly (ε-caprolactone) scaffolds for bone regenerationen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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