The strength of the protein-material interaction determines cell fate

González-García, Cristina; Cantini, Marco; Ballester-Beltrán, José; Altankov, George; Salmerón‐Sánchez, Manuel

doi:10.1016/j.actbio.2018.07.016

Cited by 29 publications

(28 citation statements)

References 50 publications

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“…In contrast, the MA functional group stays in a single plane and allows for better ordering of the hydrating water molecules (Figure ). Previously, we have shown experimentally that the adhesion strength of fibronectin on PMA is significantly less than that of fibronectin adsorbed on PEA, which is consistent with these simulation findings. Therefore, we conclude that FN is less likely to interact with the MA surface because the hydration layer of water molecules is more difficult to penetrate.…”

Section: Discussionsupporting

confidence: 91%

Minor Chemistry Changes Alter Surface Hydration to Control Fibronectin Adsorption and Assembly into Nanofibrils

Bieniek

Llopis-Hernández

Douglas

et al. 2019

Advcd Theory and Sims

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Fibronectin (FN) is a large glycoprotein which links and transmits signals between the cell's cytoskeleton and the extracellular matrix. FN organization into fibrils and then fibrillogenesis can be induced with the right substrate, such as poly(ethyl acrylate) (PEA), on which FN becomes extended.Interestingly, the almost identical polymer poly(methyl acrylate) (PMA), which has one less methylene bridge (─CH 2 ─), does not cause fibrillogenesis. To investigate the difference in FN behavior on PEA and PMA, the two substrates are modeled using ethyl acrylate (EA) and methyl acrylate (MA) functionalized self-assembled monolayers (SAMs). It is confirmed experimentally that the EA and MA SAMs exhibit a similar behavior in vitro to the polymers in terms of fibronectin fibrillogenesis, domain exposure, and cell adhesion. All-atom molecular dynamics simulations of the FNIII 9-10 domains interacting with each SAM show the adsorption of these two domains on EA SAMs and no adsorption on MA SAMs. Consistently, the experiments show that FN fibrillogenesis takes place on EA SAMs but not on MA SAMs. It is found that the extra methylene group in the EA headgroup leads to more motion within the headgroup that results in a markedly less dense hydration layer, which facilitates FN fibrillogenesis.

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Section: Discussionsupporting

confidence: 91%

Minor Chemistry Changes Alter Surface Hydration to Control Fibronectin Adsorption and Assembly into Nanofibrils

Bieniek

Llopis-Hernández

Douglas

et al. 2019

Advcd Theory and Sims

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“…In fact, although all samples with PCL exhibited some sort of reticular protein structure after rinsing the serum with saline buffer, the surface onAPsIPN80 was the only one barely influenced by the deposition of proteins. The shape and distribution of this type of lattices is known to determine the functional domains revealed to the vicinities, the cue for cells’ fate when seeded on this type of substrates [ 36 , 37 ].…”

Section: Discussionmentioning

confidence: 99%

Amphipathic Substrates Based on Crosslinker-Free Poly(ε-Caprolactone):Poly(2-Hydroxyethyl Methacrylate) Semi-Interpenetrated Networks Promote Serum Protein Adsorption

Vilariño-Feltrer

Salgado-Gallegos

de-la-Concepción-Ausina

et al. 2020

Polymers

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A simple procedure has been developed to synthesize uncrosslinked soluble poly(hydroxyethyl methacrylate) (PHEMA) gels, ready for use in a subsequent fabrication stage. The presence of 75 wt % methanol (MetOH) or dimethylformamide (DMF) impedes lateral hydroxyl–hydroxyl hydrogen bonds between PHEMA macromers to form during their solution polymerization at 60 °C, up to 24 h. These gels remain soluble when properly stored in closed containers under cold conditions and, when needed, yield by solvent evaporation spontaneous physically-crosslinked PHEMA adapted to the mould used. Moreover, this two-step procedure allows obtaining multicomponent systems where a stable and water-affine PHEMA network would be of interest. In particular, amphiphilic polycaprolactone (PCL):PHEMA semi-interpenetrated (sIPN) substrates have been developed, from quaternary metastable solutions in chloroform (CHCl3):MetOH 3:1 wt. and PCL ranging from 50 to 90 wt % in the polymer fraction (thus determining the composition of the solution). The coexistence of these countered molecules, uniformly distributed at the nanoscale, has proven to enhance the number and interactions of serum protein adsorbed from the acellular medium as compared to the homopolymers, the sIPN containing 80 wt % PCL showing an outstanding development. In accordance to the quaternary diagram presented, this protocol can be adapted for the development of polymer substrates, coatings or scaffolds for biomedical applications, not relying upon phase separation, such as the electrospun mats here proposed herein (12 wt % polymer solutions were used for this purpose, with PCL ranging from 50% to 100% in the polymer fraction).

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“…Fibronectincoated AFM also demonstrated that the strength of protein material interactions determines cell fate. Stronger interactions between fibronectin and materials led to decreased cell viability by hindering matrix remodeling (González-garcía et al, 2018).…”

Section: Coated Afm: Modified Tips For Selective Protein Detectionmentioning

confidence: 99%

Controlling Experimental Parameters to Improve Characterization of Biomaterial Fouling

Jesmer

Wylie

2020

Front. Chem.

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Uncontrolled protein adsorption and cell binding to biomaterial surfaces may lead to degradation, implant failure, infection, and deleterious inflammatory and immune responses. The accurate characterization of biofouling is therefore crucial for the optimization of biomaterials and devices that interface with complex biological environments composed of macromolecules, fluids, and cells. Currently, a diverse array of experimental conditions and characterization techniques are utilized, making it difficult to compare reported fouling values between similar or different biomaterials. This review aims to help scientists and engineers appreciate current limitations and conduct fouling experiments to facilitate the comparison of reported values and expedite the development of low-fouling materials. Recent advancements in the understanding of protein–interface interactions and fouling variability due to experiment conditions will be highlighted to discuss protein adsorption and cell adhesion and activation on biomaterial surfaces.

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The strength of the protein-material interaction determines cell fate

Cited by 29 publications

References 50 publications

Minor Chemistry Changes Alter Surface Hydration to Control Fibronectin Adsorption and Assembly into Nanofibrils

Minor Chemistry Changes Alter Surface Hydration to Control Fibronectin Adsorption and Assembly into Nanofibrils

Amphipathic Substrates Based on Crosslinker-Free Poly(ε-Caprolactone):Poly(2-Hydroxyethyl Methacrylate) Semi-Interpenetrated Networks Promote Serum Protein Adsorption

Controlling Experimental Parameters to Improve Characterization of Biomaterial Fouling

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