RAFT polymerization of a RGD peptide-based methacrylamide monomer for cell adhesion

2018 ◽  
Vol 9 (14) ◽  
pp. 1780-1786 ◽  
Author(s):  
Chao Chen ◽  
San H. Thang
Keyword(s):  
Cell Adhesion ◽  
Raft Polymerization ◽  
Rgd Peptide ◽  
Robust Method ◽  
Support Cell

The present study provides a robust method for the preparation of RGD peptide-based polymers that has important implications in the synthesized biomaterials that support cell adhesion.

scholarly journals Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations.

1991 ◽  
Vol 112 (1) ◽  
pp. 169-181 ◽  
Author(s):  
M J Elices ◽  
L A Urry ◽  
M E Hemler
Keyword(s):  
Cell Adhesion ◽  
Divalent Cations ◽  
Small Cell Lung Carcinoma ◽  
Rgd Peptide ◽  
Dependent Manner ◽  
Cell Lung Carcinoma ◽  
Ligand Affinity ◽  
Rgd Site ◽  
Inhibition Studies ◽  
Laminin Binding

The capability of the integrin VLA-3 to function as a receptor for collagen (Coll), laminin (Lm), and fibronectin (Fn) was addressed using both whole cell adhesion assays and ligand affinity columns. Analysis of VLA-3-mediated cell adhesion was facilitated by the use of a small cell lung carcinoma line (NCI-H69), which expresses VLA-3 but few other integrins. While VLA-3 interaction with Fn was often low or undetectable in cells having both VLA-3 and VLA-5, NCI-H69 cells readily attached to Fn in a VLA-3-dependent manner. Both Arg-Gly-Asp (RGD) peptide inhibition studies, and Fn fragment affinity columns suggested that VLA-3, like VLA-5, may bind to the RGD site in human Fn. However, unlike Fn, both Coll and Lm supported VLA-3-mediated adhesion that was not inhibited by RGD peptide, and was totally unaffected by the presence of VLA-5. In addition, VLA-3-mediated binding to Fn was low in the presence of Ca++, but was increased 6.6-fold with Mg++, and 30-fold in the presence of Mn++. In contrast, binding to Coll was increased only 1.2-fold with Mg++, and 1.7-fold in Mn++, as compared to the level seen with Ca++. Together, these experiments indicate that VLA-3 can bind Coll, Lm, and Fn, and also show that (a) VLA-3 can recognize both RGD-dependent and RGD-independent ligands, and (b) different VLA-3 ligands have distinctly dissimilar divalent cation sensitivities.

Cellular responses to novel, micropatterned biomaterials

2008 ◽  
Vol 80 (11) ◽  
pp. 2479-2487 ◽  
Author(s):  
Marga C. Lensen ◽  
Vera A. Schulte ◽  
Jochen Salber ◽  
Mar Diez ◽  
Fabian Menges ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cellular Responses ◽  
Poly Ethylene Glycol ◽  
Uv Curable ◽  
Cellular Behavior ◽  
Remarkable Effect ◽  
Support Cell ◽  
Poly Ethylene ◽  
Line Patterns ◽  
Perfluorinated Polyether

Two UV-curable polymers, i.e., a star-shaped poly(ethylene glycol) (PEG) and a linear perfluorinated polyether (PFPE), are investigated as novel biomaterials in a systematic study of the cellular responses to surface chemistry, topography, and elasticity. Based on the wettability it was expected that the two novel biomaterials were too hydrophilic or -phobic, respectively, to support cell adhesion. Indeed, no cell adhesion was observed on the smooth, unstructured elastomers, whereas the materials showed no cytotoxicity. However, when the materials bear defined, topographic patterns (prepared by UV-based imprinting), cells do react strongly to the surfaces; they adhere, spread, and change their shape depending on the geometry of the features. Typically, cells were found to align along line patterns and "float" on pillar structures. It should be noted that the chemistry of the surface is not altered by the imprinting process, hence, there are no biofunctional molecules present at the surface to aid the cell adhesion. Finally, a remarkable effect of elasticity on the cellular behavior was discovered. Thus, the three parameters of chemistry, topography, and elasticity were investigated in- and interdependently, and it was found that the biomaterials may lose their resistance to protein adsorption and cell adhesion depending on the surface topography.

Buried, Covalently Attached RGD Peptide Motifs in Poly(methacrylic acid) Brush Layers: The Effect of Brush Structure on Cell Adhesion

Langmuir ◽  
2008 ◽  
Vol 24 (19) ◽  
pp. 10996-11002 ◽  
Author(s):  
Melba Navarro ◽  
Edmondo M. Benetti ◽  
Szczepan Zapotoczny ◽  
Josep A. Planell ◽  
G. Julius Vancso
Keyword(s):  
Cell Adhesion ◽  
Methacrylic Acid ◽  
Rgd Peptide ◽  
Peptide Motifs

Comparative cell adhesion properties of cysteine extended peptide architectures

RSC Advances ◽  
2016 ◽  
Vol 6 (4) ◽  
pp. 2695-2702 ◽  
Author(s):  
Saniye Soylemez ◽  
Bilal Demir ◽  
Gizem Oyman Eyrilmez ◽  
Seçkin Kesici ◽  
Aytül Saylam ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Attachment ◽  
Rgd Peptide ◽  
Adhesion Properties ◽  
Modified Surfaces

This study presents the comparative cell attachment investigation of TAT and well-known RGD peptide modified surfaces.

scholarly journals A Role for Tissue Factor in Cell Adhesion and Migration Mediated by Interaction with Actin-binding Protein 280

1998 ◽  
Vol 140 (5) ◽  
pp. 1241-1253 ◽  
Author(s):  
Ilka Ott ◽  
Edgar G. Fischer ◽  
Yohei Miyagi ◽  
Barbara M. Mueller ◽  
Wolfram Ruf
Keyword(s):  
Cell Adhesion ◽  
Tumor Cell ◽  
Tissue Factor ◽  
Cell Spreading ◽  
Cytoplasmic Domain ◽  
Actin Binding ◽  
Support Cell ◽  
Cell Metastasis ◽  
Tumor Cell Metastasis ◽  
And Migration

Tissue factor (TF), the protease receptor initiating the coagulation system, functions in vascular development, angiogenesis, and tumor cell metastasis by poorly defined molecular mechanisms. We demonstrate that immobilized ligands for TF specifically support cell adhesion, migration, spreading, and intracellular signaling, which are not inhibited by RGD peptides. Two-hybrid screening identified actin-binding protein 280 (ABP-280) as ligand for the TF cytoplasmic domain. Extracellular ligation of TF is necessary for ABP-280 binding. ABP-280 recruitment to TF adhesion contacts is associated with reorganization of actin filaments, but cytoskeletal adaptor molecules typically found in integrin-mediated focal contacts are not associated with TF. Chimeric molecules of the TF cytoplasmic domain and an unrelated extracellular domain support cell spreading and migration, demonstrating that the extracellular domain of TF is not involved in the recruitment of accessory molecules that influence adhesive functions. Replacement of TF's cytoplasmic Ser residues with Asp to mimic phosphorylation enhances the interaction with ABP-280, whereas Ala mutations abolish coprecipitation of ABP-280 with immobilized TF cytoplasmic domain, and severely reduce cell spreading. The specific interaction of the TF cytoplasmic domain with ABP-280 provides a molecular pathway by which TF supports tumor cell metastasis and vascular remodeling.

Dendrimer surface orientation of the RGD peptide affects mesenchymal stem cell adhesion

RSC Advances ◽  
2016 ◽  
Vol 6 (55) ◽  
pp. 49839-49844 ◽  
Author(s):  
Y. Vida ◽  
D. Collado ◽  
F. Najera ◽  
S. Claros ◽  
J. Becerra ◽  
...  
Keyword(s):  
Stem Cells ◽  
Mesenchymal Stem Cells ◽  
Stem Cell ◽  
Cell Adhesion ◽  
Mesenchymal Stem Cell ◽  
Tissue Regeneration ◽  
Surface Orientation ◽  
Rgd Peptide

Mesenchymal stem cells (MSCs) are promising candidates for a range of tissue regeneration applications.

Control of Cell Adhesion and Detachment on Temperature-Responsive Block Copolymer Langmuir Films

2014 ◽  
Vol 1621 ◽  
pp. 101-106 ◽  
Author(s):  
Morito Sakuma ◽  
Yoshikazu Kumashiro ◽  
Masamichi Nakayama ◽  
Nobuyuki Tanaka ◽  
Umemura Kazuo ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Block Copolymer ◽  
Raft Polymerization ◽  
Langmuir Films ◽  
Chemical Compositions ◽  
Langmuir Film ◽  
Atomic Force ◽  
Responsive Surfaces ◽  
Modified Surface ◽  
Response To Temperature

ABSTRACTThis study used Langmuir-Schaefer (LS) method to produce thermo-responsive poly(N-isopropylacrylamide) (PIPAAm) modified surface. Block copolymer composed of polystyrene (PSt) and PIPAAm was synthesized by RAFT polymerization. PSt-block-PIPAAm (St-IP) with various chemical compositions was dropped on an air-water interface and formed Langmuir film by compression. Then, the Langmuir film changing a density was transferred on a hydrophobic modified glass substrate to produce St-IP transferred surface (St-IP LS surface). From the observation of atomic force microscope images, a nanostructure was observed on the transference of Langmuir films. Cell adhesion and detachment were also evaluated on the LS surfaces in response to temperature. Cell adhesion on LS surfaces at 37 °C was controlled by changing the chemical compositions and densities. After reducing temperature to 20 °C, adhering cells rapidly detached themselves with lower Am and higher composition of PIPAAm. Our method should be proved novel insights for investigating cell adhesion and detachment on thermo-responsive surfaces.

Endothelial cell adhesion and blood response to hemocompatible peptide 1 (HCP-1), REDV, and RGD peptide sequences with free N-terminal amino groups immobilized on a biomedical expanded polytetrafluorethylene surface

2021 ◽  
Author(s):  
Yihua Liu ◽  
Atsushi Mahara ◽  
Yusuke Kambe ◽  
Yu-I. Hsu ◽  
Tetsuji Yamaoka
Keyword(s):  
Cell Adhesion ◽  
Endothelial Cell ◽  
Rgd Peptide ◽  
Terminal Cell ◽  
Amino Groups ◽  
Cell Adhesive ◽  
Terminal Amino ◽  
Endothelial Cell Adhesion

Free N-terminal cell adhesive peptides are assessed from the viewpoint of endothelial cell adhesion and blood response.

The extracellular matrix (mesoglea) of hydrozoan jellyfish and its ability to support cell adhesion and spreading

Hydrobiologia ◽  
1991 ◽  
Vol 216-217 (1) ◽  
pp. 3-10 ◽  
Author(s):  
V. Schmid ◽  
A. Bally ◽  
K. Beck ◽  
M. Haller ◽  
W. K. Schlage ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Support Cell

Movable Polyrotaxane Surfaces for Modulating Cellular Adhesion via Specific RGD-Integrin Binding

2012 ◽  
Vol 86 ◽  
pp. 59-62
Author(s):  
Ji Hun Seo ◽  
Sachiro Kakinoki ◽  
Tetsuji Yamaoka ◽  
Nobuhiko Yui
Keyword(s):  
Cell Adhesion ◽  
Click Reaction ◽  
Cellular Adhesion ◽  
Important Variable ◽  
Rgd Peptide ◽  
Bioactive Molecules ◽  
Biological Responses ◽  
Cell Adhesive ◽  
Rigid Surfaces ◽  
Chemical Groups

Immobilizing bioactive molecules on the materials surfaces is one of the main strategies for creating functional bio-interfaces. In these kinds of bio-interfaces, the density of immobilized functional groups and the following physicochemical factors such as roughness, polarity and electrical charge have been thought important variables for regulating biological responses such as cell adhesion and differentiations. Here in this study, differences between rigidity and dynamically immobilized bioactive molecules on the biological responses will be discussed. In order to develop dynamic bio-interfaces, a polyrotaxane based block-copolymer containing clickable azide groups for conjugating various bioactive molecules was designed. Cell adhesive RGD peptide was then conjugated with the azide group by click reaction on both dynamic and rigid surfaces. As a result, cell adhesive RGD peptide immobilized on the dynamic bio-interfaces shows larger initial cell adhesion area, indicating that molecular dynamics of surface chemical groups is another important variable for the regulation of biological responses.

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