A chimeric peptide that binds to titanium and mediates MC3T3-E1 cell adhesion

Wang, Dan; Mao, Jing; Zhou, Bin; Liao, Xiao‐Fu; Shuili, Gong; Liu, Yan; Zhang, Jingtao

doi:10.1007/s10529-010-0411-9

Cited by 11 publications

(7 citation statements)

References 18 publications

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“…Osteoblasts express a variety of extracellular markers, including integrins, which allow binding with surrounding proteins containing RGD recognition sites . A chimeric peptide consisting of an RGD sequence and RKLPDA was used to mediate MC3T3‐E1 cell adhesion . The RGD motif is one of the most studied integrin‐stimulating peptides.…”

Section: Discussionmentioning

confidence: 99%

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RGD‐modified dihydrolipoamide dehydrogenase as a molecular bridge for enhancing the adhesion of bone forming cells to titanium dioxide implant surfaces

Dayan¹,

Lamed²,

Benayahu

et al. 2018

J Biomedical Materials Res

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Titanium and its alloys are widely used in dental‐ and orthopedic implants, the outer surface of which is often oxidized to titanium dioxide (TiO2). To achieve efficient osseointegration with bone‐forming cells, it is desirable to counter the formation of the soft fibrous tissue around the implant by creating strong and stable interactions between the implant surface and bone‐forming osteoblasts. To address this challenge, a bioactive coating had to be designed. Protein adsorption to TiO2 is well known in the literature, but it is mostly characterized by weak associations, rendering less efficient implant osseointegration. We have previously demonstrated the unique conjugation between the dihydrolipoamide dehydrogenase (DLDH) protein and TiO2 surfaces, based on specific coordinative bonding via Cys–His–Glu–Asp motif residues. To enhance cell binding to DLDH and facilitate osseointegration, DLDH was bioengineered to include Arg–Gly–Asp (RGD) moieties (DLDHRGD). Coating TiO2 disks with DLDHRGD led to improved adherence of integrin‐expressing osteogenic MBA‐15 to the surface of the disks. Following the enhanced adsorption, higher proliferation rates of the adherent cells, as well as faster mineralization were observed, compared to controls. © 2018 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 107A: 545–551, 2019.

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Section: Discussionmentioning

confidence: 99%

“…24 A chimeric peptide consisting of an RGD sequence and RKLPDA was used to mediate MC3T3-E1 cell adhesion. 45 The RGD motif is one of the most studied integrin-stimulating peptides. This sequence is a ubiquitous adhesive motif that is found in many bone ECM glycoproteins.…”

Section: Discussionmentioning

confidence: 99%

RGD‐modified dihydrolipoamide dehydrogenase as a molecular bridge for enhancing the adhesion of bone forming cells to titanium dioxide implant surfaces

Dayan¹,

Lamed²,

Benayahu

et al. 2018

J Biomedical Materials Res

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“…Beide fördern die Zelladhäsion [77,78], die Daten zum Einfluss auf die Knochenheilung sind allerdings auch hier widersprüchlich. In manchen Studien zeigte P15 einen positiven Effekt auf die Osseointegration [79], der sich in anderen Studien nicht bestätigte [80].…”

Section: Peptide Aus Knochenmatrixproteinenunclassified

“…Eine Technik beschreibt die Anwendung von chimären Peptiden zur Verbesserung der Zelladhäsion, in denen die RGD-mit einer RKLPDA-Sequenz kombiniert ist, die an Titan binden kann [78]. Es wurde auch ein Unterschied in der Wirkung von linearem und zyklischem RGD-Peptid gezeigt; Letzteres hatte einen stärkeren Einfluss auf die Zelladhäsion [77].…”

Section: Peptide Aus Knochenmatrixproteinenunclassified

Implantatoberflächen und ihr Einfluss auf das periimplantäre Hartgewebe

2014

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“…In our previous study, a novel chimeric peptide RKLPDAPRGDN (minTBP-1-PRGDN) was synthesized by connecting minTBP-1 to the N-terminal of PRGDN. This chimeric peptide was found to exhibit favorable affinity for the Ti surface and the modified Ti was associated with improved attachment and spreading of MC3T3-E1 cells (9).…”

Section: Introductionmentioning

confidence: 99%

A novel chimeric peptide binds MC3T3-E1 cells to titanium and enhances their proliferation and differentiation

Wang

Liao

et al. 2013

Molecular Medicine Reports

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Previous studies have demonstrated that the modification of the titanium (Ti) surface of an implant with RGD (Arg‑Gly‑Asp) promotes the activity of osteoblasts. A novel Ti‑binding peptide, minTBP‑1, and a chimeric peptide, minTBP‑1‑PRGDN, have been synthesized to assist the fixing of RGD to Ti. In our previous study, minTBP‑1‑PRGDN demonstrated favorable affinity for Ti surfaces and facilitated the adhesion of MC3T3‑E1 cells. The aim of the present study was to evaluate the effect of this chimeric peptide on the proliferation and differentiation of MC3T3‑E1 cells. For this purpose, MC3T3‑E1 cells were cultured and differentiation was induced on Ti discs precoated with minTBP‑1‑PRGDN, minTBP‑1 or PRGDN. The MC3T3‑E1 cells on the minTBP‑1‑PRGDN‑precoated Ti disc were observed to exhibit the highest cell number after 24 h and alkaline phosphatase levels in all groups increased in a time‑dependent manner. In addition, marked expression of osteogenic marker genes [osteopontin (OPN) and osteocalcin (OC)] was detected on minTBP‑1‑PRGDN/Ti at day 14. Mineralized deposits on minTBP‑1‑PRGDN/Ti presented the maximal average area and the highest number of deposits was observed on PRGDN/Ti. The present study indicates that minTBP‑1‑PRGDN may enhance and accelerate the activities of MC3T3‑E1 cells on Ti, however, its role in vivo must be determined by further studies.

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A chimeric peptide that binds to titanium and mediates MC3T3-E1 cell adhesion

Cited by 11 publications

References 18 publications

RGD‐modified dihydrolipoamide dehydrogenase as a molecular bridge for enhancing the adhesion of bone forming cells to titanium dioxide implant surfaces

RGD‐modified dihydrolipoamide dehydrogenase as a molecular bridge for enhancing the adhesion of bone forming cells to titanium dioxide implant surfaces

Implantatoberflächen und ihr Einfluss auf das periimplantäre Hartgewebe

A novel chimeric peptide binds MC3T3-E1 cells to titanium and enhances their proliferation and differentiation

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