The Experts below are selected from a list of 39102 Experts worldwide ranked by ideXlab platform
Alan J Grodzinsky - One of the best experts on this subject based on the ideXlab platform.
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sustained delivery of bioactive tgf β1 from self assembling Peptide hydrogels induces chondrogenesis of encapsulated bone marrow stromal cells
Journal of Biomedical Materials Research Part A, 2014Co-Authors: Paul W Kopesky, John D Kisiday, Sangwon Byun, Eric J Vanderploeg, David D Frisbie, Alan J GrodzinskyAbstract:Tissue engineering strategies for cartilage defect repair require technology for local targeted delivery of chondrogenic and anti-inflammatory factors. The objective of this study was to determine the release kinetics of transforming growth factor β1 (TGF-β1) from Self-Assembling Peptide hydrogels, a candidate scaffold for cell transplant therapies, and stimulate chondrogenesis of encapsulated young equine bone marrow stromal cells (BMSCs). Although both Peptide and agarose hydrogels retained TGF-β1, 5-fold higher retention was found in Peptide. Excess unlabeled TGF-β1 minimally displaced retained radiolabeled TGF-β1, demonstrating biologically relevant loading capacity for Peptide hydrogels. The initial release from acellular Peptide hydrogels was nearly 3-fold lower than agarose hydrogels, at 18% of loaded TGF-β1 through 3 days as compared to 48% for agarose. At day 21, cumulative release of TGF-β1 was 32–44% from acellular Peptide hydrogels, but was 62% from Peptide hydrogels with encapsulated BMSCs, likely due to cell-mediated TGF-β1 degradation and release of small labeled species. TGF-β1 loaded Peptide hydrogels stimulated chondrogenesis of young equine BMSCs, a relevant preclinical model for treating injuries in young human cohorts. Self-Assembling Peptide hydrogels can be used to deliver chondrogenic factors to encapsulated cells making them a promising technology for in vivo, cell-based regenerative medicine.
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effects of dexamethasone on mesenchymal stromal cell chondrogenesis and aggrecanase activity comparison of agarose and self assembling Peptide scaffolds
Cartilage, 2013Co-Authors: Emily Florine, Rachel E Miller, Ryan M Porter, Christopher H Evans, Bodo Kurz, Alan J GrodzinskyAbstract:Objective—Dexamethasone (Dex) is a synthetic glucocorticoid that has pro-anabolic and anticatabolic effects in cartilage tissue engineering systems, though the mechanisms by which these effects are mediated are not well understood. We tested the hypothesis that the addition of Dex to chondrogenic medium would affect matrix production and aggrecanase activity of human and bovine bone marrow stromal cells (BMSCs) cultured in Self-Assembling Peptide and agarose hydrogels. Design—We cultured young bovine and adult human BMSCs in (RADA)4 Self-Assembling Peptide and agarose hydrogels in medium containing TGF-β1±Dex and analyzed extracellular matrix composition, aggrecan cleavage products, and the effects of the glucocorticoid receptor antagonist RU-486 on proteoglycan content, synthesis, and catabolic processing.
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controlled delivery of transforming growth factor β1 by self assembling Peptide hydrogels induces chondrogenesis of bone marrow stromal cells and modulates smad2 3 signaling
Tissue Engineering Part A, 2011Co-Authors: Paul W Kopesky, John D Kisiday, Eric J Vanderploeg, David D Frisbie, John D Sandy, Alan J GrodzinskyAbstract:Self-Assembling Peptide hydrogels were modified to deliver transforming growth factor β1 (TGF-β1) to encapsulated bone-marrow-derived stromal cells (BMSCs) for cartilage tissue engineering applications using two different approaches: (i) biotin-streptavidin tethering; (ii) adsorption to the Peptide scaffold. Initial studies to determine the duration of TGF-β1 medium supplementation necessary to stimulate chondrogenesis showed that 4 days of transient soluble TGF-β1 to newborn bovine BMSCs resulted in 10-fold higher proteoglycan accumulation than TGF-β1-free culture after 3 weeks. Subsequently, BMSC-seeded Peptide hydrogels with either tethered TGF-β1 (Teth-TGF) or adsorbed TGF-β1 (Ads-TGF) were cultured in the TGF-β1-free medium, and chondrogenesis was compared to that for BMSCs encapsulated in unmodified Peptide hydrogels, both with and without soluble TGF-β1 medium supplementation. Ads-TGF Peptide hydrogels stimulated chondrogenesis of BMSCs as demonstrated by cell proliferation and cartilage-like extra...
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self assembling Peptide hydrogel fosters chondrocyte extracellular matrix production and cell division implications for cartilage tissue repair
Proceedings of the National Academy of Sciences of the United States of America, 2002Co-Authors: John D Kisiday, Shuguang Zhang, Carlos E Semino, Bodo Kurz, H Hung, Alan J GrodzinskyAbstract:Emerging medical technologies for effective and lasting repair of articular cartilage include delivery of cells or cell-seeded scaffolds to a defect site to initiate de novo tissue regeneration. Biocompatible scaffolds assist in providing a template for cell distribution and extracellular matrix (ECM) accumulation in a three-dimensional geometry. A major challenge in choosing an appropriate scaffold for cartilage repair is the identification of a material that can simultaneously stimulate high rates of cell division and high rates of cell synthesis of phenotypically specific ECM macromolecules until repair evolves into steady-state tissue maintenance. We have devised a Self-Assembling Peptide hydrogel scaffold for cartilage repair and developed a method to encapsulate chondrocytes within the Peptide hydrogel. During 4 weeks of culture in vitro, chondrocytes seeded within the Peptide hydrogel retained their morphology and developed a cartilage-like ECM rich in proteoglycans and type II collagen, indicative of a stable chondrocyte phenotype. Time-dependent accumulation of this ECM was paralleled by increases in material stiffness, indicative of deposition of mechanically functional neo-tissue. Taken together, these results demonstrate the potential of a Self-Assembling Peptide hydrogel as a scaffold for the synthesis and accumulation of a true cartilage-like ECM within a three-dimensional cell culture for cartilage tissue repair.
Shuguang Zhang - One of the best experts on this subject based on the ideXlab platform.
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lipid like self assembling Peptide nanovesicles for drug delivery
ACS Applied Materials & Interfaces, 2014Co-Authors: Dimitrios G Fatouros, Shuguang Zhang, Ioannis S. Vizirianakis, Dimitrios A Lamprou, Andrew J Urquhart, S N Yannopoulos, Sotirios KoutsopoulosAbstract:Amphiphilic Self-Assembling Peptides are func- tional materials, which, depending on the amino acid sequence, the Peptide length, and the physicochemical conditions, form a variety of nanostructures including nanovesicles, nanotubes, and nanovalves. We designed lipid- like Peptides with an aspartic acid or lysine hydrophilic head and a hydrophobic tail composed of six alanines (i.e., ac-A6K- CONH2 ,K A 6-CONH2, ac-A6D-COOH, and DA6-COOH). The resulting novel Peptides have a length similar to biological lipids and form nanovesicles at physiological conditions. AFM microscopy and light scattering analyses of the positively charged lipid-like ac-A6K-CONH2 ,K A6-CONH2 Peptide formulations showed individual nanovesicles. The negatively charged ac-A6D- COOH and DA6-COOH Peptides self-assembled into nanovesicles that formed clusters that upon drying were organized into necklace-like formations of nanovesicles. Encapsulation of probe molecules and release studies through the Peptide bilayer suggest that Peptide nanovesicles may be good candidates for sustained release of pharmaceutically active hydrophilic and hydrophobic compounds. Lipid-like Peptide nanovesicles represent a paradigm shifting system that may complement liposomes for the delivery of diagnostic and therapeutic agents.
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in vivo studies on angiogenic activity of two designer self assembling Peptide scaffold hydrogels in the chicken embryo chorioallantoic membrane
Nanoscale, 2012Co-Authors: Xiumei Wang, Akihiro Horii, Xiujuan Wang, Lin Qiao, Shuguang ZhangAbstract:The rapid promotion of angiogenesis is critical for tissue engineering and regenerative medicine. The angiogenic activity of tissue-engineered scaffolds has already been the major criterion for choosing and designing ideal biological materials. We here report systematic in vivo studies on the angiogenic activity of two functionalized Self-Assembling Peptides PRG (Ac-(RADA)4GPRGDSGYRGDS-CONH2) and KLT (Ac-(RADA)4G4KLTWQELYQLKYKGI-CONH2) using the chicken embryo chorioallantoic membrane (CAM) assay. 3D migration/sprouting bead assays showed that the two functional motifs PRGDSGYRGDS and KLTWQELYQLKYKGI improved the bioactivities of the Self-Assembling Peptide RADA16-I (Ac-(RADA)4-CONH2) dramatically and provided ideal synthetic microenvironments for endothelial cell migration and cordlike structure sprout formation. A CAM assay was carried out to assess the efficiency of various Peptide scaffolds in inducing capillary invasion in vivo. Among these three Peptide scaffolds, the functionalized Peptide scaffold RAD/KLT presented a significantly better angiogenic activity inducing CAM tissue invasion and new capillary vessel formation within the scaffolds in the absence of VEGF. With the addition of VEGF, more newly formed vessel lumen could be observed in all Peptide scaffolds. Our results suggested that the functionalized Peptide scaffolds had satisfactory angiogenic properties, and may also have wide potential applications in tissue regeneration.
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controlled release of functional proteins through designer self assembling Peptide nanofiber hydrogel scaffold
Proceedings of the National Academy of Sciences of the United States of America, 2009Co-Authors: Sotirios Koutsopoulos, Yusuke Nagai, Larry D Unsworth, Shuguang ZhangAbstract:The release kinetics for a variety of proteins of a wide range of molecular mass, hydrodynamic radii, and isoelectric points through a nanofiber hydrogel scaffold consisting of designer Self-Assembling Peptides were studied by using single-molecule fluorescence correlation spectroscopy (FCS). In contrast to classical diffusion experiments, the single-molecule approach allowed for the direct determination of diffusion coefficients for lysozyme, trypsin inhibitor, BSA, and IgG both inside the hydrogel and after being released into the solution. The results of the FCS analyses and the calculated pristine in-gel diffusion coefficients were compared with the values obtained from the Stokes–Einstein equation, Fickian diffusion models, and the literature. The release kinetics suggested that protein diffusion through nanofiber hydrogels depended primarily on the size of the protein. Protein diffusivities decreased, with increasing hydrogel nanofiber density providing a means of controlling the release kinetics. Secondary and tertiary structure analyses and biological assays of the released proteins showed that encapsulation and release did not affect the protein conformation and functionality. Our results show that this biocompatible and injectable designer Self-Assembling Peptide hydrogel system may be useful as a carrier for therapeutic proteins for sustained release applications.
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designer functionalized self assembling Peptide nanofiber scaffolds for growth migration and tubulogenesis of human umbilical vein endothelial cells
Soft Matter, 2008Co-Authors: Xiumei Wang, Akihiro Horii, Shuguang ZhangAbstract:We previously reported a class of designer Self-Assembling Peptide nanofiber scaffolds as a unique biological material for diverse applications including 3-D tissue cell culture, slow drug release, regenerative medicine, and tissue engineering. One of these Peptide scaffolds, RADA16-I has been used in bone, cartilage, and neural regeneration studies that have shown great promises. We here report the development of two new functionalized Self-Assembling Peptide nanofiber scaffolds designed specifically for angiogenesis study through directly coupling pure RADA16-I with short biologically angiogenic motifs. Angiogenesis is very important in regenerative medicine. An adequate blood vessel supply to the newly formed tissue and within the transplanted scaffold is essential in determining the success of new tissue regeneration. In our study, two designer functionalized Peptides, KLT, Ac–(RADA)4G4KLTWQELYQLKYKGI–CONH2 and PRG, Ac–(RADA)4GPRGDSGYRGDS–CONH2 significantly enhanced endothelial cell survival, proliferation, migration, and morphological tubulogenesis compared with unmodified RADA16-I scaffold. We also showed in our clear-boundary sandwich culture without adding extract soluble growth factors that cells migrated uni-directionally from RADA16-I toward the functionalized scaffolds but not the reverse. Our results suggest that the functionalized designer Peptide scaffolds will not only have great promise for promoting endothelial cell growth, migration, and tubulogenesis, but also may have widely potential applications for diverse tissue engineering and tissues regeneration.
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biological designer self assembling Peptide nanofiber scaffolds significantly enhance osteoblast proliferation differentiation and 3 d migration
PLOS ONE, 2007Co-Authors: Akihiro Horii, Xiumei Wang, Fabrizio Gelain, Shuguang ZhangAbstract:A class of Self-Assembling Peptide nanofiber scaffolds has been shown to be an excellent biological material for 3-dimension cell culture and stimulating cell migration into the scaffold, as well as for repairing tissue defects in animals. We report here the development of several Peptide nanofiber scaffolds designed specifically for osteoblasts. We designed one of the pure Self-Assembling Peptide scaffolds RADA16-I through direct coupling to short biologically active motifs. The motifs included osteogenic growth Peptide ALK (ALKRQGRTLYGF) bone-cell secreted-signal Peptide, osteopontin cell adhesion motif DGR (DGRGDSVAYG) and 2-unit RGD binding sequence PGR (PRGDSGYRGDS). We made the new Peptide scaffolds by mixing the pure RAD16 and designer-Peptide solutions, and we examined the molecular integration of the mixed nanofiber scaffolds using AFM. Compared to pure RAD16 scaffold, we found that these designer Peptide scaffolds significantly promoted mouse pre-osteoblast MC3T3-E1 cell proliferation. Moreover, alkaline phosphatase (ALP) activity and osteocalcin secretion, which are early and late markers for osteoblastic differentiation, were also significantly increased. We demonstrated that the designer, Self-Assembling Peptide scaffolds promoted the proliferation and osteogenic differentiation of MC3T3-E1. Under the identical culture medium condition, confocal images unequivocally demonstrated that the designer PRG Peptide scaffold stimulated cell migration into the 3-D scaffold. Our results suggest that these designer Peptide scaffolds may be very useful for promoting bone tissue regeneration.
Mingyao Liu - One of the best experts on this subject based on the ideXlab platform.
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self assembling Peptide based nanoparticles enhance cellular delivery of the hydrophobic anticancer drug ellipticine through caveolae dependent endocytosis
Nanomedicine: Nanotechnology Biology and Medicine, 2012Co-Authors: Shanyu Fung, Hong Yang, Mingyao Liu, Roli Bawa, Atsushi Shiozaki, Gang Zheng, Shaf KeshavjeeAbstract:Abstract A special class of Self-Assembling Peptide (EAK16-II) has been found to stabilize the hydrophobic anticancer agent ellipticine (EPT) in aqueous solution. In this study, the mechanism of such Peptide-EPT complexes to enhance cellular delivery and anticancer activity was evaluated. Results revealed that EAK16-II can form nanoparticles with EPT, having an average size of ∼100 nm. This nanoformulation had cytotoxicity to human lung carcinoma A549 cells that was comparable to EPT dissolved in dimethyl sulfoxide. It enhanced EPT uptake drastically when compared to the microformulation. Such enhanced uptake was significantly reduced by inhibitors specifically for the caveolae-dependent pathway. We also found both protonated and neutral forms of EPT present in the cells. Interestingly, both were found in the cytoplasm, co-localized with LysoTracker, whereas only protonated EPT was seen in the nucleus. The promising therapeutic efficacy, specific delivery pathway, and intracellular distribution pattern discovered in this work may help further develop EPT as a nanoformulation for clinical applications. From the Clinical Editor A special class of Self-Assembling Peptide (EAK16-II) has been found to stabilize ellipticine in aqueous solution. The authors demonstrate therapeutic efficacy, describe specific delivery pathways, and effective intracellular distribution pattern, which will aid the development of this technology for future clinical applications.
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self assembling Peptide as a potential carrier for hydrophobic anticancer drug ellipticine complexation release and in vitro delivery
Advanced Functional Materials, 2009Co-Authors: Shanyu Fung, Hong Yang, Priya T Bhola, Parisa Sadatmousavi, Edward Muzar, Mingyao Liu, P ChenAbstract:The Self-Assembling Peptide EAK16-II is capable of stabilizing hydrophobic compounds to form microcrystal suspensions in aqueous solution. Here, the ability of this Peptide to stabilize the hydrophobic anticancer agent ellipticine is investigated. The formation of Peptide-ellipticine suspensions is monitored with time until equilibrium is reached. The equilibration time is found to be dependent on the Peptide concentration. When the Peptide concentration is close to its critical aggregation concentration, the equilibration time is minimal at 5 h. With different combinations of EAK16-II and ellipticine concentrations, two molecular states (protonated or cyrstalline) of ellipticine could be stabilized. These different states of ellipticine significantly affect the release kinetics of ellipticine from the Peptide-ellipticine complex into the egg phosphatidylcholine vesicles, which are used to mimic cell membranes. The transfer rate of protonated ellipticine from the complex to the vesicles is much faster than that of crystalline ellipticine. This observation may also be related to the size of the resulting complexes as revealed from the scanning electron micrographs. In addition, the complexes with protonated ellipticine are found to have a better anticancer activity against two cancer cell lines, A549 and MCF-7. This work forms the basis for studies of the Peptide-ellipticine suspensions in vitro and in vivo leading to future development of Self-Assembling Peptide-based delivery of hydrophobic anticancer drugs.
P Chen - One of the best experts on this subject based on the ideXlab platform.
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self assembling Peptide based nanoparticles enhance anticancer effect of ellipticine in vitro and in vivo
International Journal of Nanomedicine, 2012Co-Authors: Parisa Sadatmousavi, Rong Wang, Yongfang Yuan, P ChenAbstract:BACKGROUND AND METHODS Applications of the anticancer agent, ellipticine, have been limited by its hydrophobicity and toxicity. An efficient delivery system is required to exploit the enormous potential of this compound. Recently, EAK16-II, an ionic-complementary, Self-Assembling Peptide, has been found to stabilize ellipticine in aqueous solution. Here, the anticancer activity of ellipticine encapsulated in EAK16-II (EAK-EPT) was evaluated in vitro and in vivo. RESULTS Our cellular uptake, toxicity, and apoptosis results in an A549 human lung carcinoma cell line indicate that EAK-EPT complexes are significantly more effective than treatment with EAK16-II or ellipticine alone. This is due to the ability of EAK16-II to stabilize ellipticine in a protonated state in well formed nanostructures approximately 200 nm in size. In vivo observations in an A549 nude mouse tumor model show higher antitumor activity and lower cytotoxicity of EAK-EPT complexes than in the control group treated with ellipticine alone. Tumor growth in animals was significantly inhibited after treatment with EAK-EPT complexes, and without any apparent side effects. CONCLUSION The anticancer activity observed in this study coupled with minimal side effects encourages further development of Peptide-mediated delivery of anticancer drugs, ellipticine in the present case, for clinical application.
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self assembling Peptide as a potential carrier for hydrophobic anticancer drug ellipticine complexation release and in vitro delivery
Advanced Functional Materials, 2009Co-Authors: Shanyu Fung, Hong Yang, Priya T Bhola, Parisa Sadatmousavi, Edward Muzar, Mingyao Liu, P ChenAbstract:The Self-Assembling Peptide EAK16-II is capable of stabilizing hydrophobic compounds to form microcrystal suspensions in aqueous solution. Here, the ability of this Peptide to stabilize the hydrophobic anticancer agent ellipticine is investigated. The formation of Peptide-ellipticine suspensions is monitored with time until equilibrium is reached. The equilibration time is found to be dependent on the Peptide concentration. When the Peptide concentration is close to its critical aggregation concentration, the equilibration time is minimal at 5 h. With different combinations of EAK16-II and ellipticine concentrations, two molecular states (protonated or cyrstalline) of ellipticine could be stabilized. These different states of ellipticine significantly affect the release kinetics of ellipticine from the Peptide-ellipticine complex into the egg phosphatidylcholine vesicles, which are used to mimic cell membranes. The transfer rate of protonated ellipticine from the complex to the vesicles is much faster than that of crystalline ellipticine. This observation may also be related to the size of the resulting complexes as revealed from the scanning electron micrographs. In addition, the complexes with protonated ellipticine are found to have a better anticancer activity against two cancer cell lines, A549 and MCF-7. This work forms the basis for studies of the Peptide-ellipticine suspensions in vitro and in vivo leading to future development of Self-Assembling Peptide-based delivery of hydrophobic anticancer drugs.
John D Kisiday - One of the best experts on this subject based on the ideXlab platform.
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sustained delivery of bioactive tgf β1 from self assembling Peptide hydrogels induces chondrogenesis of encapsulated bone marrow stromal cells
Journal of Biomedical Materials Research Part A, 2014Co-Authors: Paul W Kopesky, John D Kisiday, Sangwon Byun, Eric J Vanderploeg, David D Frisbie, Alan J GrodzinskyAbstract:Tissue engineering strategies for cartilage defect repair require technology for local targeted delivery of chondrogenic and anti-inflammatory factors. The objective of this study was to determine the release kinetics of transforming growth factor β1 (TGF-β1) from Self-Assembling Peptide hydrogels, a candidate scaffold for cell transplant therapies, and stimulate chondrogenesis of encapsulated young equine bone marrow stromal cells (BMSCs). Although both Peptide and agarose hydrogels retained TGF-β1, 5-fold higher retention was found in Peptide. Excess unlabeled TGF-β1 minimally displaced retained radiolabeled TGF-β1, demonstrating biologically relevant loading capacity for Peptide hydrogels. The initial release from acellular Peptide hydrogels was nearly 3-fold lower than agarose hydrogels, at 18% of loaded TGF-β1 through 3 days as compared to 48% for agarose. At day 21, cumulative release of TGF-β1 was 32–44% from acellular Peptide hydrogels, but was 62% from Peptide hydrogels with encapsulated BMSCs, likely due to cell-mediated TGF-β1 degradation and release of small labeled species. TGF-β1 loaded Peptide hydrogels stimulated chondrogenesis of young equine BMSCs, a relevant preclinical model for treating injuries in young human cohorts. Self-Assembling Peptide hydrogels can be used to deliver chondrogenic factors to encapsulated cells making them a promising technology for in vivo, cell-based regenerative medicine.
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controlled delivery of transforming growth factor β1 by self assembling Peptide hydrogels induces chondrogenesis of bone marrow stromal cells and modulates smad2 3 signaling
Tissue Engineering Part A, 2011Co-Authors: Paul W Kopesky, John D Kisiday, Eric J Vanderploeg, David D Frisbie, John D Sandy, Alan J GrodzinskyAbstract:Self-Assembling Peptide hydrogels were modified to deliver transforming growth factor β1 (TGF-β1) to encapsulated bone-marrow-derived stromal cells (BMSCs) for cartilage tissue engineering applications using two different approaches: (i) biotin-streptavidin tethering; (ii) adsorption to the Peptide scaffold. Initial studies to determine the duration of TGF-β1 medium supplementation necessary to stimulate chondrogenesis showed that 4 days of transient soluble TGF-β1 to newborn bovine BMSCs resulted in 10-fold higher proteoglycan accumulation than TGF-β1-free culture after 3 weeks. Subsequently, BMSC-seeded Peptide hydrogels with either tethered TGF-β1 (Teth-TGF) or adsorbed TGF-β1 (Ads-TGF) were cultured in the TGF-β1-free medium, and chondrogenesis was compared to that for BMSCs encapsulated in unmodified Peptide hydrogels, both with and without soluble TGF-β1 medium supplementation. Ads-TGF Peptide hydrogels stimulated chondrogenesis of BMSCs as demonstrated by cell proliferation and cartilage-like extra...
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self assembling Peptide hydrogel fosters chondrocyte extracellular matrix production and cell division implications for cartilage tissue repair
Proceedings of the National Academy of Sciences of the United States of America, 2002Co-Authors: John D Kisiday, Shuguang Zhang, Carlos E Semino, Bodo Kurz, H Hung, Alan J GrodzinskyAbstract:Emerging medical technologies for effective and lasting repair of articular cartilage include delivery of cells or cell-seeded scaffolds to a defect site to initiate de novo tissue regeneration. Biocompatible scaffolds assist in providing a template for cell distribution and extracellular matrix (ECM) accumulation in a three-dimensional geometry. A major challenge in choosing an appropriate scaffold for cartilage repair is the identification of a material that can simultaneously stimulate high rates of cell division and high rates of cell synthesis of phenotypically specific ECM macromolecules until repair evolves into steady-state tissue maintenance. We have devised a Self-Assembling Peptide hydrogel scaffold for cartilage repair and developed a method to encapsulate chondrocytes within the Peptide hydrogel. During 4 weeks of culture in vitro, chondrocytes seeded within the Peptide hydrogel retained their morphology and developed a cartilage-like ECM rich in proteoglycans and type II collagen, indicative of a stable chondrocyte phenotype. Time-dependent accumulation of this ECM was paralleled by increases in material stiffness, indicative of deposition of mechanically functional neo-tissue. Taken together, these results demonstrate the potential of a Self-Assembling Peptide hydrogel as a scaffold for the synthesis and accumulation of a true cartilage-like ECM within a three-dimensional cell culture for cartilage tissue repair.