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Delforge, Dominique; Gillon, Barbara; Art, Muriel; Dewelle, Janique; Raes, Martine; Remacle, José

doi:10.1023/a:1008880124720

Cited by 4 publications

(4 citation statements)

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“…These techniques aim at the creation of artificial biomimetic surfaces through the incorporation of bioadhesive motifs from the extracellular matrix proteins. Beside the binding of peptide sequences, [6][7][8][9][10][11] the research has focused on implant precoating with proteins such as elastin, fibronectin, vitronectin, laminin, or collagen, which include multiple binding patterns supporting attachment of various integrin and nonintegrin receptors, located at the cell membrane. Binding activates signaling pathways able to stimulate cell adhesion, migration, proliferation, differentiation, or matrix mineralization.…”

Section: Introductionmentioning

confidence: 99%

Molecular Dynamics Simulations of Collagen-like Peptide Adsorption on Titanium-Based Material Surfaces

Monti

2007

J. Phys. Chem. C

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Classical molecular dynamics simulations were performed to investigate the early processes taking place in the interface region between titanium dioxide and a type I collagen triple helical segment, rich in hydroxyproline and proline residues, with special focus on intermolecular interactions and conformational stability. Possible binding modes were identified, and the analysis of the structural macroscopic and microscopic properties succeeded in elucidating the behavior of the helical bundle in contact with the TiO 2 layer. The stability of the adsorbed molecules increased with the increasing number of coordinated atoms, and side-chain groups seemed to be primarily responsible of the adsorption process. However, a certain degree of disruption of the bundle was observed and quantified, considering the interchain distances and total solvent-exposed surface area. The results were consistent with previous studies and experimental data, which revealed that major changes in collagen conformation took place in water solution.

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Section: Introductionmentioning

confidence: 99%

Molecular Dynamics Simulations of Collagen-like Peptide Adsorption on Titanium-Based Material Surfaces

Monti

2007

J. Phys. Chem. C

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“…Building block C is a bioactive domain. The central area of this domain is made up of the RGD loop of human fibronectin, (AVTG RGD SPASS), which contains the well-known integrin-mediated cell adhesion tripeptide RGD. , The whole RGD loop found in the natural protein, rather than just the bioactive tripeptide, was included in this design to mimic the occurrence of this bioactive motif in natural proteins because it is known that the whole loop adopts a folded structure that helps the RGD motif to be more accessible for cell interactions. − This central domain is flanked by two (VPGIG) 10 wings in building block C. VPGIG is similar to VPGVG, but the second l -valine of the latter has been replaced by l -isoleucine, which is slightly more hydrophobic but maintains the LCST behavior and antifouling properties . This building block is therefore markedly amphiphilic as the RGD loop is clearly hydrophilic and contains several amino acids whose side chains are hydrophilic or even charged at physiological pH, whereas the VPGIG wings are somewhat apolar and show LCST behavior.…”

Section: Resultsmentioning

confidence: 99%

Efficient Cell and Cell-Sheet Harvesting Based on Smart Surfaces Coated with a Multifunctional and Self-Organizing Elastin-Like Recombinamer

et al. 2013

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A wide range of smart surfaces with novel properties relevant for biomedical applications have been developed recently. Herein we focus on thermoresponsive surfaces that switch between cell-adherent and nonadherent states and their applications for cell harvesting. These smart surfaces are obtained by covalently coupling a tailored elastin-like recombinamer onto glass surfaces by means of the well-known and widely applied Click Chemistry methodology. The resulting recombinamer-functionalized surfaces have been characterized by means of water contact angle measurements, XPS and TOF-SIMS. A cell-based analysis of these surfaces with human fibroblasts showed a high degree of adhesion to the surface in its adherent state (37 °C), thus, promoting cell viability and proliferation. A temperature decrease triggers reorganization of the recombinamer, thus, markedly increasing the number of nonadherent domains and masking the adherent ones. This process allows a specific and efficient temporal control of cell adhesion and cell detachment. After determination of the properties required for a suitable cell-harvesting system, optimization of the process allows single cells or cell sheets from at least two types of cells (HFF-1 and ADSCs) to be rapidly harvested.

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“…The surfaces on which the coating is formed may be 2-dimensional flat sheets or 3-dimensional porous networks. 1 Peptides of vastly different sizes have been utilised as coatings from the minimal tripeptide sequence 2 to entire proteins containing 3,4 or grafted with [5][6][7] the active sequence. The amount of RGD peptides coated onto surfaces can be controlled by the concentration of the coating solution.…”

Section: Coatingsmentioning

confidence: 99%