Effect of biomaterial surface properties on fibronectin–α5β1 integrin interaction and cellular attachment

Lee, Mark H.; Ducheyne, Paul; Lynch, Laura; Boettiger, David; Composto, Russell J.

doi:10.1016/j.biomaterials.2005.11.003

Cited by 172 publications

(174 citation statements)

References 52 publications

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“…Treatment of microfluidic channels with Pluronic has similarly demonstrated lower aggregation of complexes, evidenced by a homogeneous layer of deposited lipoplexes [18]. Alternatively, the presence of EG groups could be preventing complex unfolding, as conformational changes are widely reported at surfaces for other macromolecules [56][57][58]. This change in complex morphology on SAMs containing EG terminal functional groups correlates with high transfection levels and transfection efficiencies, and could indicate the ability of EG-containing SAMs to preserve complex morphology upon binding by limiting electrostatic interactions with the surface and reducing aggregation of the complexes through steric stabilization, or alternatively by preventing complex unfolding, which could also contribute to the large height and area-perimeter ratios of the complexes immobilized on surfaces without EG.…”

Section: Atomic Force Microscopy Imaging Of Immobilized Complexesmentioning

confidence: 99%

Surface polyethylene glycol enhances substrate-mediated gene delivery by nonspecifically immobilized complexes

2008

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Substrate-mediated gene delivery describes the immobilization of gene therapy vectors to a biomaterial, which enhances gene transfer by exposing adhered cells to elevated DNA concentrations within the local microenvironment. Surface chemistry has been shown to affect transfection by nonspecifically immobilized complexes using self-assembled monolayers (SAMs) of alkanethiols on gold. In this report, SAMs were again used to provide a controlled surface to investigate whether the presence of oligo(ethylene glycol) (EG) groups in a SAM could affect complex morphology and enhance transfection. EG groups were included at percentages that did not affect cell adhesion. Nonspecific complex immobilization to SAMs containing combinations of EG-and carboxylic acidterminated alkanethiols resulted in substantially greater transfection than surfaces containing no EG groups or SAMs composed of EG groups combined with other functional groups. Enhancement in transfection levels could not be attributed to complex binding densities or release profiles. Atomic force microscopy imaging of immobilized complexes revealed that EG groups within SAMs affected complex size and appearance and could indicate the ability of these surfaces to preserve complex morphology upon binding. The ability to control the morphology of the immobilized complexes and influence transfection levels through surface chemistry could be translated to scaffolds for gene delivery in tissue engineering and diagnostic applications.

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Section: Atomic Force Microscopy Imaging Of Immobilized Complexesmentioning

confidence: 99%

Surface polyethylene glycol enhances substrate-mediated gene delivery by nonspecifically immobilized complexes

2008

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“…The influence of surface chemistry on protein adsorption and cell adhesion has been addressed mostly on surfaces with well controlled chemistry, in order to investigate the role of concrete chemical groups in self-assembly monolayers SAM (e.g. OH, COOH, NH 2 , CH 3 and their mixtures) Keselowsky et al, 2004;Faucheux et al;Lee et al, 2006;Barrias et al, 2009). Studies on fibronectin (FN) and vitronectin (VN) adsorption under non-competitive and competitive (multi-protein solutions, including FBS) conditions suggested the major role of VN in cell-materials interaction.…”

Section: Substrate Engineeringmentioning

confidence: 99%

Cell-Protein-Material Interaction in Tissue Engineering

Salmerón‐Sánchez¹,

Altankov²

2010

Tissue Engineering

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“…After fabrication, GPTMS samples were immersed in 2.75 mM β-mercaptoethanol (βME) in phosphate buffer solution (PBS, pH 7.4) for 16 h and sonicated twice with ultrapure H 2 O to produce OH SAMs. [17] Peptide-immobilized substrates were fabricated using an adaptation of the protocol used by Xiao et al [18] APTES SAMs were immersed and sonicated in 5.0 mM solution of β-Corresponding author; E-mail address: markhl@alumni.upenn.edu The concentration of the peptide solution was varied to achieve the same surface density (6 pmol/cm 2 ), as determined from radiolabeling results. Unreacted maleimides were subsequently blocked using a 1mM βME solution in PBS for 30 min.…”

Section: Substrate Preparationmentioning

confidence: 99%

“…The protocol for radiolabeling of affinity-purified human plasma fibronectin (Fn) is described in detail elsewhere. [17,21] confluency) and had enough room to spread and proliferate. The cells were allowed to attach in serum-free medium overnight (12 h); this was replaced with complete medium at day 1.…”

Section: Determination Of Peptide Surface Densitymentioning

confidence: 99%

Adhesion of MC3T3‐E1 cells to RGD peptides of different flanking residues: Detachment strength and correlation with long‐term cellular function

Lee

Adams

Boettiger

et al. 2006

J Biomedical Materials Res

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We synthesized a series of RGD peptides and immobilized them to an amine-functional self-assembled monolayer using a modified maleimide-based conjugate technique that minimizes nonspecific interactions. Using a spinning disc apparatus, a trend in the detachment strength (τ 50 ) of RGD peptides of different flanking residues was found: RGDSPK ≻ RGDSVVYGLR ≈ RGDS ≻ RGES. Using blocking monoclonal antibodies, cellular adhesion to the peptides was shown to be primarily α √ -integrin-mediated. In contrast, the τ 50 value of the cells on fibronectin (Fn)-coated substrates of similar surface density was 6-7 times higher and involved both α 5 β 1 and α ν β 3 integrins. Cellular spreading was enhanced on RGD peptides after 1 h when compared to RGE and unmodified substrates. However, no significant differences were observed between the different RGD peptides. Long-term function of MC3T3-E1 cells was also evaluated by measuring alkaline phosphatase (ALP) activity and mineral deposition. Among the four peptides, RGDSPK exhibited the highest level of ALP activity after 11 days and mineralization after 15 days and reached comparable levels as Fn substrates after 15 and 24 days, respectively. These findings collectively illustrate both the advantages and limitations of enhancing cellular adhesion and function by the design of RGD peptides. AbstractWe synthesized a series of RGD peptides and immobilized them to an amine-functional selfassembled monolayer using a modified maleimide-based conjugate technique which minimizes non-specific interactions. Using a spinning disc apparatus, a trend in the detachment strength (τ 50 ) of RGD peptides of different flanking residues was found: RGDSPK > RGDSVVYGLR ≈ RGDS > RGES. Using blocking monoclonal antibodies, cellular adhesion to the peptides was shown to be primarily α v -integrin-mediated. In contrast, the τ 50 value of the cells on fibronectin (Fn) coated substrates of similar surface density was 6-7 times higher and involved both α 5 β 1 and α v β 3 integrins. Cellular spreading was enhanced on RGD peptides after 1 h in comparison to RGE and unmodified substrates. However, no significant differences were observed between the different RGD peptides. Long-term function of MC3T3-E1 cells was also evaluated by measuring alkaline phosphatase (ALP) activity and mineral deposition. Among the four peptides, RGDSPK exhibited the highest level of ALP activity after 11 days and mineralization after 15 days and reached comparable levels as Fn substrates after 15 and 24 days respectively.These findings collectively illustrate both the advantages and limitations of enhancing cellular adhesion and function by the design of RGD peptides.

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Effect of biomaterial surface properties on fibronectin–α5β1 integrin interaction and cellular attachment

Cited by 172 publications

References 52 publications

Surface polyethylene glycol enhances substrate-mediated gene delivery by nonspecifically immobilized complexes

Surface polyethylene glycol enhances substrate-mediated gene delivery by nonspecifically immobilized complexes

Cell-Protein-Material Interaction in Tissue Engineering

Adhesion of MC3T3‐E1 cells to RGD peptides of different flanking residues: Detachment strength and correlation with long‐term cellular function

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