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

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.

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.

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.

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.

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.

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.

Effect of cyclic RGD peptide on cell adhesion and tumor metastasis

1991 ◽  
Vol 177 (1) ◽  
pp. 74-82 ◽  
Author(s):  
Hiromichi Kumagai ◽  
Mayumi Tajima ◽  
Yukio Ueno ◽  
Yuhko Giga-Hama ◽  
Masataka Ohba
Keyword(s):  
Cell Adhesion ◽  
Tumor Metastasis ◽  
Rgd Peptide
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