Porous protein–silica composite formation: manipulation of silicate porosity and protein conformation

Fournier, Agathe C.; McGrath, Kathryn M.

doi:10.1039/c1sm05299c

Cited by 9 publications

(6 citation statements)

References 47 publications

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“…Next we determined to localize within the PROP which His residues/clusters bind to the silica surface. From studies using bovine serum albumin and lysozyme, it has been established that α–helices bind to silica monoliths . During binding to those surfaces, the conformation changes and the ordered α–helix content decreases, with the result that the proteins become more disordered.…”

Section: Discussionmentioning

confidence: 99%

The silicatein propeptide acts as inhibitor/modulator of self‐organization during spicule axial filament formation

et al. 2013

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Silicateins are crucial enzymes that are involved in formation of the inorganic biosilica scaffold of the spicular skeleton of siliceous sponges. We show that silicatein acquires its structure-guiding and enzymatically active state by processing of silicatein from pro-silicatein to the mature enzyme. A recombinant propeptide (PROP) of silicatein from the siliceous demosponge Suberites domuncula was prepared, and antibodies were raised against the peptide. In sponge tissue, these antibodies reacted with both surface structures and the central region of the spicules. Using phage display expression, spicule-binding 12-mer peptides were identified that are rich in histidine residues. In the predicted tertiary structure of PROP, these histidine residues are only present in the a-helical region. The recombinant PROP was found to inhibit self-assembly of silicatein molecules. By light scattering, it was shown that, in the presence of 4 M urea, the recombinant silicatein is obtained in the mono/oligomeric form with a hydrodynamic radius of 4 nm, while lower urea concentrations promote self-aggregation and assembly of the protein. Finally, it is shown that the enzymatic activity of silicatein is abolished by PROP in silicatein samples that predominantly contain mono-or oligomeric silicatein particles, but the enzyme is not affected if present in the filamentous aggregated form. It is concluded that the functions of silicatein, acting as a structural template for its biosilica product and as an enzyme, are modulated and controlled by its propeptide. Structured digital abstractalpha-silicatein and alpha-silicatein bind by transmission electron microscopy (View interaction)[Structured digital abstract was added on 27 March 2013 after original online publication]

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Section: Discussionmentioning

confidence: 99%

The silicatein propeptide acts as inhibitor/modulator of self‐organization during spicule axial filament formation

et al. 2013

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“…Since BSA nanoparticles present a porous structure, silica precursors penetrate easily into the nanoparticles, then, nucleation and assembly of silica take place inside the nanoparticles [27]. It seems that BSA provides an environment that facilitates silica nucleation and growth of the particles, probably due to the functional groups of BSA that could associate with silica through hydrogen bonding and electrostatic interactions [50]. During the growth of silica, BSA protein is entrapped into the silica framework.…”

Section: Resultsmentioning

confidence: 99%

Protein-Silica Hybrid Submicron Particles: Preparation and Characterization

et al. 2020

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Purpose Hybrid nanoparticles are an interesting type of particles currently employed in nanomedicine. They can combine the therapeutic and diagnostic functions of their components into one single nanosystem and therefore, can be tweaked according to their applications and desired results. The purpose of this work is to develop an easily tuned nano-system of bovine serum albumin-silica hybrid nanoparticles. Methods BSA nanoparticles were prepared by nanoprecipitation process using water as the solvent phase and ethanol as the non-solvent. Silica was produced through a sol-gel process and deposited inside the BSA nanoparticles via template deposition. The effect of initial concentrations of raw materials on the structure and colloidal properties of the system was evaluated using FTIR, TGA, TEM, and zeta potential measurements. Results A hybrid structure of BSA-silica was obtained. The results suggest that the particles size, isoelectric point and silica content of the hybrid nanoparticles can be easily tuned by controlling adequately the concentration of TEOS and ammonia. Conclusion Our method can be considered as a novel approach for hybrid nanoparticle synthesis. To our knowledge, we report for the first time the synthesis of silica-BSA hybrid particles with a non-core-shell structure. In addition, we proved that that the particles size, isoelectric point and silica content of the hybrid nanoparticles can be easily tuned by controlling adequately the concentration of TEOS and ammonia.

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“…In aqueous solution, the deprotonation of silanol (SiOH) groups into SiO − results in a highly polar bond. The electronegative oxygen atom in SiO − can interact with the basic amino acid residues in proteins such as guanidinium or NH

_{3}^{+}

, resulting in hydrogen bonding (NH ··· O) between the substrate and the protein 48, 49. Another material related parameter that could contribute to the enhanced protein adsorption to SCPC50 is the high surface area provided by the porosity of the surface.…”

Section: Discussionmentioning

confidence: 99%

Promotion of pro‐osteogenic responses by a bioactive ceramic coating

Aniket

Young

Marriott

et al. 2012

J Biomedical Materials Res

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The objective of this study was to analyze the responses of bone-forming osteoblasts to Ti-6Al-4V implant material coated with silica-calcium phosphate nanocomposite (SCPC50). Osteoblast differentiation at the interface with SCPC50-coated Ti-6Al-4V was correlated to the adsorption of high amount of serum proteins, high surface affinity to fibronectin, Ca uptake from and P and Si release into the medium. SCPC50-coated Ti-6Al-4V adsorbed significantly more serum protein (p < 0.05) than control uncoated substrates. Moreover, Western blot analysis showed that the SCPC50 coating had a high affinity for serum fibronectin. Protein conformation analyses by FTIR showed that the ratio of the area under the peak for amide I/amide II bands was significantly higher (p < 0.05) on the surface of SCPC50-coated substrates than that on the surface of the control uncoated substrates. Moreover, ICP À OES analyses indicated that SCPC50-coated substrates withdrew Ca ions from, and released P and Si ions into, the tissue culture medium, respectively. In conjunction with the favorable protein adsorption and modifications in medium composition, MC3T3-E1 osteoblast-like cells attached to SCPC50coated substrates expressed 10-fold higher level of mRNA encoding osteocalcin and had significantly higher production of osteopontin and osteocalcin proteins than cells attached to the uncoated Ti-6A1-4V substrates. In addition, osteoblast-like cells attached to the SCPC50-coated substrates produced significantly lower levels of the inflammatory and osteoclastogenic cytokines, IL-6, IL-12p40, and RANKL than those attached to uncoated Ti-6Al-4V substrates. These results suggest that SCPC50 coating could enhance bone integration with orthopedic and maxillofacial implants while minimizing the induction of inflammatory bone cell responses. V

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Porous protein–silica composite formation: manipulation of silicate porosity and protein conformation

Cited by 9 publications

References 47 publications

The silicatein propeptide acts as inhibitor/modulator of self‐organization during spicule axial filament formation

The silicatein propeptide acts as inhibitor/modulator of self‐organization during spicule axial filament formation

Protein-Silica Hybrid Submicron Particles: Preparation and Characterization

Promotion of pro‐osteogenic responses by a bioactive ceramic coating

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