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Journal ArticleDOI

RGD modified polymers: biomaterials for stimulated cell adhesion and beyond

Ulrich Hersel, +2 more
- 01 Nov 2003 - 
- Vol. 24, Iss: 24, pp 4385-4415
TLDR
The impacts of RGD peptide surface density, spatial arrangement as well as integrin affinity and selectivity on cell responses like adhesion and migration are discussed.
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This article is published in Biomaterials.The article was published on 2003-11-01. It has received 2443 citations till now. The article focuses on the topics: Cell adhesion & Adhesion.

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Citations
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Journal ArticleDOI

Kinetic behaviour of the cells touching substrate: the interfacial stiffness guides cell spreading.

TL;DR: Based on simulation analyses, the elasticity of silica-like layer induced by UV radiation on PDMS surface dominated cell-substrate interaction, rather than the bulk stiffness of the material, indicating that it is the interfacial stiffness that mainly guided the cell spreading.
Journal ArticleDOI

Cell adhesion on an artificial extracellular matrix using aptamer-functionalized PEG hydrogels

TL;DR: It is shown that nucleic acid aptamers could be incorporated into polyethylene glycol (PEG) hydrogels via free radical polymerization and cell adhesion to the aptamer-functionalized hydrogel could be attenuated by means of aptamer inactivation in a physiological condition.
Journal ArticleDOI

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

TL;DR: Iniferter-mediated surface-initiated photopolymerization was used to graft poly(methacrylic acid) brush layers obtained from surface-attached iniferters in self-assembled monolayers to a gold surface, and immunofluorescence studies demonstrated a variation of the cell morphology as a function of the position of the peptide units along the grafted chains.
Journal ArticleDOI

Osteogenic Differentiation of Human Mesenchymal Stem Cells Directed by Extracellular Matrix-Mimicking Ligands in a Biomimetic Self-Assembled Peptide Amphiphile Nanomatrix

TL;DR: Overall, the PA nanomatrix clearly has great promise for directing the osteogenic differentiation of hMSCs without the aid of supplements by mimicking the native ECM, providing an adaptable environment that allows for different adhesive ligands to control cellular behaviors.
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Functionalizing αvβ3- or α5β1-selective integrin antagonists for surface coating: a method to discriminate integrin subtypes in vitro

TL;DR: A strategy to synthesize avb3or a5b1specific ligands for the functionalization of nanostructured gold surfaces is reported and it is demonstrated that cell adhesion can be selectively mediated by a single integrin subtype.
References
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Journal ArticleDOI

New perspectives in cell adhesion : RGD and integrins

TL;DR: Together, the adhesion proteins and their receptors constitute a versatile recognition system providing cells with anchorage, traction for migration, and signals for polarity, position, differentiation, and possibly growth.
Journal ArticleDOI

Geometric control of cell life and death.

TL;DR: Human and bovine capillary endothelial cells were switched from growth to apoptosis by using micropatterned substrates that contained extracellular matrix-coated adhesive islands of decreasing size to progressively restrict cell extension.
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Polyvalent Interactions in Biological Systems: Implications for Design and Use of Multivalent Ligands and Inhibitors.

TL;DR: Polyvalent interactions can be collectively much stronger than corresponding monovalent interactions, and they can provide the basis for mechanisms of both agonizing and antagonizing biological interactions that are fundamentally different from those available inmonovalent systems.
Journal ArticleDOI

Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule

TL;DR: The ability of fibronectin to bind cells can be accounted for by the tetrapeptide L-arginyl-glycyl- L-aspartyl-L-serine, a sequence which is part of the cell attachment domain of fibronsectin and present in at least five other proteins.
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