Sustained delivery of PlGF-2123-144*-fused BMP2-related peptide P28 from small intestinal submucosa/polylactic acid scaffold material for bone tissue regeneration. Issue 12 (19th February 2020)
- Record Type:
- Journal Article
- Title:
- Sustained delivery of PlGF-2123-144*-fused BMP2-related peptide P28 from small intestinal submucosa/polylactic acid scaffold material for bone tissue regeneration. Issue 12 (19th February 2020)
- Main Title:
- Sustained delivery of PlGF-2123-144*-fused BMP2-related peptide P28 from small intestinal submucosa/polylactic acid scaffold material for bone tissue regeneration
- Authors:
- Xiong, Zekang
Cui, Wei
Sun, Tingfang
Teng, Yu
Qu, Yanzhen
Yang, Liang
Zhou, Jinge
Chen, Kaifang
Yao, Sheng
Shao, Zengwu
Guo, Xiaodong - Abstract:
- Abstract : Sustained delivery of PlGF-2123-144* -fused BMP2-related peptide P28 from SIS/PLA scaffold facilitate the adhesion, proliferation, and osteogenic differentiation of bone marrow stromal cells. This system effectively promotes segmental bone repair. Abstract : Bone morphogenetic protein 2 (BMP-2) is one of the most important factors for bone tissue formation. However, its use over the past decade has been associated with numerous side effects. This is due to the fact that recombinant human (rh) BMP-2 has several biological functions, as well as that non-physiological high dosages were commonly administered. In this study, we synthesized a novel BMP-2-related peptide (designated P28) and fused a mutant domain in placenta growth factor-2 (PlGF-2123-144* ) that allowed for the "super-affinity" of extracellular matrix proteins to P28, effectively controlling the release of low dosage P28 from small intestinal submucosa/polylactic acid (SIS/PLA) scaffolds. These have been shown to be excellent scaffold materials both in vivo and in vitro . The aim of this study was to determine whether these scaffolds could support the controlled release of P28 over time, and whether the composite materials could serve as structurally and functionally superior bone substitutes in vivo . Our results demonstrated that P28 could be released slowly from SIS/PLA to promote the adhesion, proliferation, and differentiation of bone marrow stromal cells (BMSCs) in vitro . In vivo, radiographicAbstract : Sustained delivery of PlGF-2123-144* -fused BMP2-related peptide P28 from SIS/PLA scaffold facilitate the adhesion, proliferation, and osteogenic differentiation of bone marrow stromal cells. This system effectively promotes segmental bone repair. Abstract : Bone morphogenetic protein 2 (BMP-2) is one of the most important factors for bone tissue formation. However, its use over the past decade has been associated with numerous side effects. This is due to the fact that recombinant human (rh) BMP-2 has several biological functions, as well as that non-physiological high dosages were commonly administered. In this study, we synthesized a novel BMP-2-related peptide (designated P28) and fused a mutant domain in placenta growth factor-2 (PlGF-2123-144* ) that allowed for the "super-affinity" of extracellular matrix proteins to P28, effectively controlling the release of low dosage P28 from small intestinal submucosa/polylactic acid (SIS/PLA) scaffolds. These have been shown to be excellent scaffold materials both in vivo and in vitro . The aim of this study was to determine whether these scaffolds could support the controlled release of P28 over time, and whether the composite materials could serve as structurally and functionally superior bone substitutes in vivo . Our results demonstrated that P28 could be released slowly from SIS/PLA to promote the adhesion, proliferation, and differentiation of bone marrow stromal cells (BMSCs) in vitro . In vivo, radiographic and histological examination showed that SIS/PLA/P28/PlGF-2123-144* completely repaired critical-size bone defects, compared to SIS/PLA, SIS/PLA/PlGF-2123-144*, or SIS/PLA/P28 alone. These findings suggest that this controlled release system may have promising clinical applications in bone tissue engineering. … (more)
- Is Part Of:
- RSC advances. Volume 10:Issue 12(2020)
- Journal:
- RSC advances
- Issue:
- Volume 10:Issue 12(2020)
- Issue Display:
- Volume 10, Issue 12 (2020)
- Year:
- 2020
- Volume:
- 10
- Issue:
- 12
- Issue Sort Value:
- 2020-0010-0012-0000
- Page Start:
- 7289
- Page End:
- 7300
- Publication Date:
- 2020-02-19
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c9ra07868a ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 12914.xml