Open AccessSustained delivery of recombinant human bone morphogenetic protein‐2 from perlecan domain I ‐ functionalized electrospun poly (ε‐caprolactone) scaffolds for bone regeneration
Author(s) -
Chiu YuChieh,
Fong Eliza L.,
Grindel Brian J.,
Kasper Fred K.,
Harrington Daniel A.,
FarachCarson Mary C.
Publication year - 2016
Publication title -
journal of experimental orthopaedics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.597
H-Index - 18
ISSN - 2197-1153
DOI - 10.1186/s40634-016-0057-1
Subject(s) - perlecan , scaffold , chemistry , bone morphogenetic protein 2 , bone morphogenetic protein , regeneration (biology) , tissue engineering , bone healing , biomedical engineering , microbiology and biotechnology , biochemistry , heparan sulfate , anatomy , glycosaminoglycan , biology , medicine , in vitro , gene
Abstract Background 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.