A comparative study of polyethylene glycol hydrogels derivatized with the RGD peptide and the cell-binding domain of fibronectin

Zhang, Chen; Hekmatfer, Sogol; Karuri, Nancy W.

doi:10.1002/jbm.a.34687

Cited by 16 publications

(16 citation statements)

References 40 publications

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“…[22,66–68] Fewer studies have explicitly compared cell adhesion on substrates modified with either linear or cyclic RGD peptides. Those studies that have compared the different RGD conformations to each other generally find that the efficiency of cell adhesion, the degree of cell spreading, and the organization of the cytoskeleton are greater on the cyclic peptide, which has been attributed to a higher affinity of the cyclic peptide for the integrin receptor.…”

Section: Discussionmentioning

confidence: 99%

A gene expression-based comparison of cell adhesion to extracellular matrix and RGD-terminated monolayers

Sobers¹,

Wood²,

Mrksich³

2015

Biomaterials

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This work uses global gene expression analysis to compare the extent to which model substrates presenting peptide adhesion motifs mimic the use of conventional extracellular matrix protein coated substrates for cell culture. We compared the transcriptional activities of genes in cells that were cultured on matrix-coated substrates with those cultured on self-assembled monolayers presenting either a linear or cyclic RGD peptide. Cells adherent to cyclic RGD were most similar to those cultured on native ECM, while cells cultured on monolayers presenting the linear RGD peptide had transcriptional activities that were more similar to cells cultured on the uncoated substrates. This study suggests that biomaterials presenting the cyclic RGD peptide are substantially better mimics of extracellular matrix than are uncoated materials or materials presenting the common linear RGD peptide.

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Section: Discussionmentioning

confidence: 99%

A gene expression-based comparison of cell adhesion to extracellular matrix and RGD-terminated monolayers

Sobers¹,

Wood²,

Mrksich³

2015

Biomaterials

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“…This is consistent with the rather dense structure of Multilayer‐3M, which is composed of almost equal amounts of PSS and PDADMAC, and thereby will block the penetration of larger molecules such as Fn. Compared with Multilayer‐5M with the highest swelling, the less swollen Multilayer‐1M adsorbed the largest amount of Fn, revealing that the surface charge has an important role as well …”

Section: Resultsmentioning

confidence: 99%

“…Here, the relative activity of RGD, the major active domain of Fn, was analyzed by ELISA. As the Fn molecule interacts with the integrin α 5 β 1 or α v β 3 of cells via their RGD domain, it is valid to conclude that the RGD activity and the Fn functionality are directly related. Figure b reveals that the relative activity of RGD was highest for the Fn molecules adsorbed on Multilayer‐1M and 3M from 10% FBS, and lowest on Multilayer‐5M.…”

Section: Resultsmentioning

confidence: 99%

Adsorption of Fibronectin on Salt-Etched Polyelectrolyte Multilayers and its Roles in Mediating the Adhesion and Migration of Vascular Smooth Muscle Cells

et al. 2014

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Protein adsorption on biomaterials strongly mediates the subsequent cell responses. Here adsorption of fibronectin (Fn) on salt-treated PEI(PSS/PDDA)7 multilayers was characterized. The amounts of adsorbed Fn increased linearly along with the increase of thickness of multilayers pretreated with 1 M and 5 M NaCl solutions (Multilayer-1M and 5M), but was independent on the thickness of Multilayer-3M. The normalized relative RGD activity of Fn were significantly higher on the Multilayer-3M than on others. By comparison of cellular behaviors of VSMCs being cultured in the normal and Fn-depleted serum-containing medium, the significant role of Fn on modulating the behaviors of VSMCs was verified. The Fn adsorption model and its role on linking the biomaterials surface to the VSMCs behaviors are proposed.

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“…Adhesion assays were carried out using established methods . Glass coverslips in a 24 well plate were incubated in 50 μg/mL native or PEGylated FN in PBS.…”

Section: Methodsmentioning

confidence: 99%

Proteolytically stabilizing fibronectin without compromising cell and gelatin binding activity

Zhang

Ramanathan

Karuri

2014

Biotechnology Progress

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Excessive proteolytic degradation of fibronectin (FN) has been implicated in impaired tissue repair in chronic wounds. We previously reported two strategies for stabilizing FN against proteolytic degradation; the first conjugated polyethylene glycol (PEG) through cysteine residues and the second conjugated PEG chains of varying molecular weight on lysine residues. PEGylation of FN via lysine residues resulted in increased resistance to proteolysis with increasing PEG size, but an overall decrease in biological activity, as characterized by cell and gelatin binding. Our latest method to stabilize FN against proteolysis masks functional regions in the protein during lysine PEGylation. FN is PEGylated while it is bound to gelatin Sepharose beads with 2, 5, and 10 kDa PEG precursors. This results in partially PEGylated FN that is more stable than native FN and whose proteolytic stability increases with PEG molecular weight. Unlike completely PEGylated FN, partially PEGylated FN has cell adhesion, gelatin binding, and matrix assembly responses that are comparable to native FN. This is new evidence of how PEGylation variables can be used to stabilize FN while retaining its activity. The conjugates developed herein can be used to dissect molecular mechanisms mediated by FN stability and functionality, and address the problem of FN degradation in chronic wounds.

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A comparative study of polyethylene glycol hydrogels derivatized with the RGD peptide and the cell-binding domain of fibronectin

Cited by 16 publications

References 40 publications

A gene expression-based comparison of cell adhesion to extracellular matrix and RGD-terminated monolayers

A gene expression-based comparison of cell adhesion to extracellular matrix and RGD-terminated monolayers

Adsorption of Fibronectin on Salt-Etched Polyelectrolyte Multilayers and its Roles in Mediating the Adhesion and Migration of Vascular Smooth Muscle Cells

Proteolytically stabilizing fibronectin without compromising cell and gelatin binding activity

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