NTA-Co3+-His6 versus NTA-Ni2+-His6 mediated E-Cadherin surface immobilization enhances cellular traction

Russo, Jacopo Di; Young, Jennifer L.; Balakrishnan, Adithya; Benk, Amelie S.; Spatz, Joachim P.

doi:10.1016/j.biomaterials.2018.10.042

Cited by 10 publications

(7 citation statements)

References 34 publications

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“…First, using the very same surface chemistry, the surface density of biomolecules immobilized onto TiO 2 was found to be higher than that onto Au, with values of 130 and 30 fmol/mm 2 for TiO 2 and Au, respectively . In both cases, the surface density is higher than the reported threshold of 1 fmol/mm 2 of cell adhesion molecules sufficient to promote adhesion and spreading for both integrin-mediated and cadherin-mediated adhesions . Remarkably, this threshold was established based on arrays of segregated ligands separated by tens of nanometers, whereas continuous layers were used in the present case, and these continuous layers provide the maximal surface density of both ligands to the cells.…”

Section: Resultsmentioning

confidence: 90%

“…41 In both cases, the surface density is higher than the reported threshold of 1 fmol/ mm 2 of cell adhesion molecules sufficient to promote adhesion and spreading for both integrin-mediated 67 and cadherinmediated adhesions. 68 Remarkably, this threshold was established based on arrays of segregated ligands separated by tens of nanometers, whereas continuous layers were used in the present case, and these continuous layers provide the maximal surface density of both ligands to the cells. Importantly, this also implies that the differences in surface densities, if they exist, cannot explain alone the contact guidance on bifunctional surfaces.…”

Section: Anisotropy Of Cadherin and Cadherin−rgd Pattern Induces Cont...mentioning

confidence: 87%

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Cell–Cell Adhesion-Driven Contact Guidance and Its Effect on Human Mesenchymal Stem Cell Differentiation

Saux

Wu²,

Toledo

et al. 2020

ACS Appl. Mater. Interfaces

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Contact guidance has been extensively explored using patterned adhesion functionalities that predominantly mimic cell–matrix interactions. Whether contact guidance can also be driven by other types of interactions, such as cell−cell adhesion, still remains a question. Herein, this query is addressed by engineering a set of microstrip patterns of (i) cell–cell adhesion ligands and (ii) segregated cell–cell and cell–matrix ligands as a simple yet versatile set of platforms for the guidance of spreading, adhesion, and differentiation of mesenchymal stem cells. It was unprecedently found that micropatterns of cell–cell adhesion ligands can induce contact guidance. Surprisingly, it was found that patterns of alternating cell–matrix and cell–cell strips also induce contact guidance despite providing a spatial continuum for cell adhesion. This guidance is believed to be due to the difference between the potencies of the two adhesions. Furthermore, patterns that combine the two segregated adhesion functionalities were shown to induce more human mesenchymal stem cell osteogenic differentiation than monofunctional patterns. This work provides new insight into the functional crosstalk between cell–cell and cell–matrix adhesions and, overall, further highlights the ubiquitous impact of the biochemical anisotropy of the extracellular environment on cell function.

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Section: Resultsmentioning

confidence: 90%

Section: Anisotropy Of Cadherin and Cadherin−rgd Pattern Induces Cont...mentioning

confidence: 87%

Cell–Cell Adhesion-Driven Contact Guidance and Its Effect on Human Mesenchymal Stem Cell Differentiation

Saux

Wu²,

Toledo

et al. 2020

ACS Appl. Mater. Interfaces

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“…To ensure the sensitivity and accuracy of the diagnosis, it is necessary to remove the His-proteins first. Immobilized metal affinity chromatography (IMAC) is considered as a popular strategy to separate His-proteins because of the coordination interaction between the histidines and transition metal ions (such as Ni 2+ ). , IMAC can efficiently and selectively separate His-proteins from a complex matrix. Depending on several commonly used ligands, such as nitrilotriacetate (NTA) and iminodiacetate (IDA), Ni 2+ could be adsorbed on the surface of the prepared materials.…”

Section: Introductionmentioning

confidence: 99%

Preparation of Fe₃O₄@PMAA@Ni Microspheres towards the Efficient and Selective Enrichment of Histidine-Rich Proteins

Wang

Wei

Gao

et al. 2021

ACS Appl. Mater. Interfaces

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Magnetic material is considered to as a major concern material for the enrichment of histidine-rich proteins (Hisproteins) via metal-ion affinity. In this work, magnetic polymer microspheres with core−shell structure (Fe 3 O 4 @PMAA@Ni) were successfully prepared via reflux-precipitation polymerization followed by in situ reduction and growth of Ni 2+ . The obtained Ni nanofoams with flower-like structure and uniform pore size (3.34 nm) provided numerous binding sites for His-proteins. The adsorption performance of Fe 3 O 4 @PMAA@Ni microspheres for His-proteins was estimated via selectively separating bovine hemoglobin (BHb) and bovine serum albumin (BSA) from a matrix composed of BHb, BSA, and lysozyme (LYZ). The results indicated that Fe 3 O 4 @PMAA@Ni microspheres could efficiently and selectively separate His-proteins from the matrix, with a maximum adsorption capacity of ∼2660 mg/g for BHb. Moreover, Fe 3 O 4 @PMAA@Ni microspheres exhibited good stability and recyclability for BHb separation over seven cycles. Therefore, this work reported a novel and facile strategy to prepare core−shell Fe 3 O 4 @PMAA@Ni microspheres, which was promising for practical applications of His-protein separation and purification in proteomics.

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“…Poly-histidine chains form a stronger and less labile coordinate bond with NTA-Co 3+ compared to the corresponding bond with NTA-Ni 2+ . 29–31…”

Section: Introductionmentioning

confidence: 99%

“…Poly-histidine chains form a stronger and less labile coordinate bond with NTA-Co 3+ compared to the corresponding bond with NTA-Ni 2+ . [29][30][31] Fig. 1: Cartoon depicting the lipid bilayer composed of POPC, cholesterol, and DGS-NTA(Ni) or NTA lipid, which acts as an anchor for a poly-histidine chain.…”

Section: Introductionmentioning

confidence: 99%

Binding of His-tagged fluorophores to lipid bilayers of giant vesicles†

Pramanik

Steinkühler²,

Dimova

et al. 2022

Preprint

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His-tagged molecules can be attached to lipid bilayers via certain anchor lipids, a method that has been widely used for the biofunctionalization of membranes and vesicles. To measure the coverage by the membrane-bound molecules, it is useful to study molecules that are fluorescent as well. Here, we use two such molecules, green fluorescence protein (GFP) and green-fluorescent fluorescin isothiocyanate (FITC), both of which are tagged with a chain of six histidines that bind to achor lipids within the bilayers. This His-tag is much smaller in size than the GFP molecule but somewhat larger than the FITC dye. The lipid bilayers form giant unilamellar vesicles (GUVs), the behavior of which can be directly observed in the optical microscope. Several protocols for the preparation of GUVs have been developed. We apply and compare three well-established protocols based on polyvinyl alcohol (PVA) hydrogel swelling, electroformation on platinum wires, and electroformation on indium tin oxide (ITO) glass. For the same nanomolar concentration in the exterior solution, the coverage by His-tagged FITC is much lower than the one by His-tagged GFP. However, for both GFP and FITC, we find that the binding of the His-tagged molecules to the anchor lipids depends strongly on the preparation method. The highest binding affinitiy is obtained for electroformation on platinum wires. PVA gel swelling gives rise to a somewhat smaller binding affinity whereas electroformation on ITO glass leads to essentially no binding. Furthermore, the binding affinitiy is also observed to depend on the pH of the aqueous solution, with a relatively weak and strong pH-dependence for His-tagged GFP and His-tagged FITC, respectively.

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NTA-Co3+-His6 versus NTA-Ni2+-His6 mediated E-Cadherin surface immobilization enhances cellular traction

Cited by 10 publications

References 34 publications

Cell–Cell Adhesion-Driven Contact Guidance and Its Effect on Human Mesenchymal Stem Cell Differentiation

Cell–Cell Adhesion-Driven Contact Guidance and Its Effect on Human Mesenchymal Stem Cell Differentiation

Preparation of Fe₃O₄@PMAA@Ni Microspheres towards the Efficient and Selective Enrichment of Histidine-Rich Proteins

Binding of His-tagged fluorophores to lipid bilayers of giant vesicles†

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NTA-Co3+-His6 versus NTA-Ni2+-His6 mediated E-Cadherin surface immobilization enhances cellular traction

Cited by 10 publications

References 34 publications

Cell–Cell Adhesion-Driven Contact Guidance and Its Effect on Human Mesenchymal Stem Cell Differentiation

Cell–Cell Adhesion-Driven Contact Guidance and Its Effect on Human Mesenchymal Stem Cell Differentiation

Preparation of Fe3O4@PMAA@Ni Microspheres towards the Efficient and Selective Enrichment of Histidine-Rich Proteins

Binding of His-tagged fluorophores to lipid bilayers of giant vesicles†

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Preparation of Fe₃O₄@PMAA@Ni Microspheres towards the Efficient and Selective Enrichment of Histidine-Rich Proteins