ArticleClinical orthopaedics and related research2011
Growth factor delivery through self-assembling peptide scaffolds.
Article in Clinical orthopaedics and related research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 35 citations in OpenAlex.
- Synthetic extracellular matrices with function-encoding peptides.Nature reviews bioengineering · 2023Review
- Self-Assembling Hydrogel Structures for Neural Tissue Repair.ACS biomaterials science & engineering · 2021Review
- Hydrogel-Based Controlled Delivery Systems for Articular Cartilage Repair.BioMed research international · 2016Article
- Controlled Angiogenesis in Peptide Nanofiber Composite Hydrogels.ACS biomaterials science & engineering · 2015Article
- Strategies for controlled delivery of biologics for cartilage repair.Advanced drug delivery reviews · 2015Review
- Expression, isolation, and purification of soluble and insoluble biotinylated proteins for nerve tissue regeneration.Journal of visualized experiments : JoVE · 2014Article
- Self-assembling peptide scaffolds as innovative platforms for drug and cell delivery systems in cardiac regeneration.Drug delivery and translational research · 2013Article
- Article
- Modulation of chondrocyte behavior through tailoring functional synthetic saccharide-peptide hydrogels.Biomaterials · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
backgroundThe best strategy for delivering growth factors to cells for the purpose of cartilage tissue engineering remains an unmet challenge. Tethering biotinylated insulin-like growth factor-1 (bIGF-1) to the self-assembling peptide scaffold (RADA)(4) effectively delivers bioactive bIGF-1 to cardiac tissue. QUESTIONS/PURPOSES: We therefore asked whether: (1) soluble bIGF-1 could stimulate proteoglycan production by chondrocytes; (2) bIGF-1 could be adsorbed or tethered to the self-assembling peptide scaffold (KLDL)(3); (3) adsorbed or tethered bIGF-1 could stimulate proteoglycan production; and (4) transforming growth factor-β1 (TGF-β1) could be adsorbed or tethered and stimulate proteoglycan production by bone marrow stromal cells (BMSCs).
methodsChondrocytes or BMSCs were encapsulated in (KLDL)(3). The growth factors were (1) delivered solubly in the medium; (2) adsorbed to (KLDL)(3); or (3) tethered to (KLDL)(3) through biotin-streptavidin bonds. Fluorescently tagged streptavidin was used to determine IGF-1 kinetics; sGAG and DNA content was measured.
resultsSoluble bIGF-1 stimulated comparable sGAG accumulation as soluble IGF-1. Tethering IGF-1 to (KLDL)(3) increased retention of IGF-1 in (KLDL)(3) compared with adsorption, but neither method increased sGAG or DNA accumulation above control. Adsorbing TGF-β1 increased proteoglycan accumulation above control, but tethering did not affect sGAG levels.
conclusionsAlthough TGF-β1 can be effectively delivered by adsorption to (KLDL)(3), IGF-1 cannot. Additionally, although tethering these factors provided long-term sequestration, tethering did not stimulate proteoglycan production. CLINICAL RELEVANCE: Tethering growth factors to (KLDL)(3) results in long-term delivery, but tethering does not necessarily result in the same bioactivity as soluble delivery, indicating presentation of proteins is vital when considering a delivery strategy.
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Registered trials
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