Ionic liquid-functionalized crystals of barium sulfate: A hybrid organic–inorganic material with tuned hydrophilicity and solid–liquid behavior

Kowacz, Magdalena; Marchel, Mateusz; Esperança, José M. S. S.; Rebelo, Luís Paulo N.

doi:10.1016/j.matchemphys.2015.04.042

Cited by 8 publications

(10 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Such a scenario is supported by recent findings showing that the driving mechanism for binding of ligands to proteins or self-assembly of folded proteins (creation of intermolecular contacts) is determined by the tendency of unsatisfied hydrogen-bonding sites at the protein surface to dehydrate upon contact formation. , Thus, the driving force encouraging protein partitioning to the solid substrate can result from the stabilization of the protein surface-exposed hydrogen-bonding sites upon hydrogen-bond formation with the inorganic solid. This mechanism of interaction corroborates the observation that the IL ions and myoglobin compete for electron-donating sites at the solid surface, as it has been recognized that ILs also bind to the surface-exposed SO 4 2– . It has been shown that amphiphilic peptides can form on charged hydrophilic surface multiple layers driven by self-association of the hydrophobic side chains in order to minimize their contact with water when the hydrophilic compartments interact with the solid .…”

Section: Discussionsupporting

confidence: 81%

“…BaSO 4 crystals were synthesized and functionalized following the procedure described in detail in our previous publication . In summary, micrometer-sized BaSO 4 (barite) crystals were precipitated by mixing aqueous solutions of BaCl 2 and Na 2 SO 4 .…”

Section: Methodsmentioning

confidence: 99%

“…The term “control conditions” used throughout the paper with respect to experiments involving proteins always designates samples without any added particles. To account for some contribution of particles to the absorbance at 280 nm, the absorbance of the samples containing particles in water only was subtracted from the protein absorption at 280 nm before calculation of the final Δ A . The absorbance coming from particles is a result of the immobilization of ILs, which if released from the surface could contribute to the absorption at 280 nm because of the presence of the imidazolium ring.…”

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Ionic-Liquid-Functionalized Mineral Particles for Protein Crystallization

Kowacz

Marchel

Juknaitė

et al. 2015

Crystal Growth & Design

View full text Add to dashboard Cite

Nucleation is a critical step determining the outcome of the entire crystallization process. Finding an effective nucleant for protein crystallization is of utmost importance for structural biology. The latter relies on good-quality crystals to solve the three-dimensional structures of macromolecules. In this study we show that crystalline barium sulfate (BaSO 4 ) with an etched and/or ionic liquid (IL)-functionalized surface (1) can induce protein nucleation at concentrations well below the concentration needed to promote crystal growth under control conditions, (2) can shorten the nucleation time, (3) can increase the growth rate, and finally (4) may help to improve the protein crystal morphology. These effects were shown for lysozyme, RNase A, trypsin, proteinase K, myoglobin, and hemoglobin. Therefore, the use of BaSO 4 particles enables us to reduce the amount of protein in crystallization trials and increases the chance of obtaining protein crystals of the desired quality. In the context of the underlying mechanism, it is shown that the protein−solid contact formation is governed by the interaction of the polar compartments of the biomacromolecule with the support. The tendency of a protein to concentrate near the solid surface is enhanced by both the hydrophobicity of the protein and that of the surface (tuned by the functionalizing IL). These mechanisms of interaction of biomacromolecules with inorganic hydrophilic solids correspond to the principles of amphiphilic IL−mineral interactions. ■ INTRODUCTIONAnalyzing protein crystals is a way to determine the threedimensional structure of the protein, which provides crucial information regarding its biological function. However, protein crystallization is still a major challenge in modern proteomics. Therefore, new and effective ways of creating good-quality protein crystals are continuously sought, and studies of the underlying mechanisms are highly desired.Heterogeneous nucleation (at some pre-existing surface) can be induced under supersaturation conditions lower than those needed for the onset of homogeneous nucleation (in the bulk of the solution). The former offers kinetic advantages and often results in crystals that are bigger and better-ordered, the characteristics that are necessary for high-resolution protein structure determination. Thus, finding an effective heterogeneous nucleant for proteins is a very promising approach, and both empirical attempts and the respective theoretical studies are constantly ongoing. 1 Works in this field have identified the features of the most successful solid nucleating agents as surface nanotopography (preferentially deep, narrow pores of wide size distribution) and/or its amorphous state. 1−6 Very recently, nonporous ordered surfaces have also been found to be prone to induce crystal growth in model systems where the crystal contacts are governed by short-range interactions (as for proteins). 7 The requirement for those surfaces to act as nucleants is the presence of surface strain. Otherwise, crystalline solids ...

show abstract

Section: Discussionsupporting

confidence: 81%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Ionic-Liquid-Functionalized Mineral Particles for Protein Crystallization

Kowacz

Marchel

Juknaitė

et al. 2015

Crystal Growth & Design

View full text Add to dashboard Cite

show abstract

“…Such considerations are in agreement with previous studies showing that mainly charged arginine provides binding sites on protein adsorption to silica nanoparticles [57] with character of those specific contacts being possibly determinative for protein functionality [58]. Yet, for patchy molecules with polar and non-polar regions it is their hydration state that defines net surface coverage developed on the solid [59]. Thus large protein-particle assemblies can be formed in solution due to dipole-like many-body interactions within this network, while packing density of individual protein coronas can be limited by shortrange hydration repulsion between immobilized proteins [15].…”

Section: Proteinsurface Interactionsupporting

confidence: 91%

Effect of Infrared Light on Protein Behavior in Contact with Solid Surface

Kowacz¹,

Warszyński²

2018

Preprint

Self Cite

View full text Add to dashboard Cite

Adsorption of proteins at a solid surface affects characteristics of the surface (e.g. its biocompatibility) and functionality of the immobilized biomacromolecules. The latter is defined by the type of binding sites, protein conformation and its structural flexibility that enable functional motions to occur. Protein motions are only possible at certain level of hydration. Furthermore, water molecules act as lubricant facilitating sliding along solid surface. In this work we explore the potential of a remote physical trigger –a non-ionizing infrared radiation (IR) to affect protein-surface interactions. We report on IR-induced changes of hydrophilicity of the protein coatings on silica nanoparticles, impact of IR on monitored in-situ dynamic adsorption of proteins on silica surface and effect of IR on conformational state of adsorbed proteins. Our results indicate that IR can protect proteins from surface denaturation depending on the presence of strongly hydrated amino acid residues. Preservation of native fold results in protein coatings of higher hydrophilicity. IR can also facilitate displacement of surface activespecies that became adsorbed to protein apolar compartments and couldotherwise promote denaturation. Apart from supporting native conformation, their removalincreases protein-water interfacial tension and therefore promotes aggregation (hydrophobic attraction) of the protein-coated nanoparticles. By its ability to affect protein conformational state and interfacial characteristics (such as effective protein-water affinity) IR radiation can therefore modulate protein interactions.

show abstract

“…Most of the polymers are hydrophobic and incompatible with the hydrophilic nanofillers. The issue of nanofiller agglomeration and weak particle-polymer affinity often lead to detrimental effects on the mechanical strength 29 – 31 . The interactions between the polymer and filler at the interface significantly influence the composite’s mechanical properties.…”

Section: Introductionmentioning

confidence: 99%

Radiopaque Fully Degradable Nanocomposites for Coronary Stents

Ang

Toong

Chow

et al. 2018

Sci Rep

View full text Add to dashboard Cite

Bioresorbable scaffolds (BRS) were introduced to overcome limitations of current metallic drug-eluting stents and poly-L-lactide (PLLA) has been used in the fabrication of BRS due to its biodegradability and biocompatibility. However, such polymers have weaker mechanical properties as compared to metals, limiting their use in BRS. We hypothesized that nanofillers can be used to enhance the mechanical properties considerably in PLLA. To this end, polymer-matrix composites consisting of PLLA reinforced with 5–20 wt% barium sulfate (BaSO4) nanofillers as a potential BRS material was evaluated. Stearic-acid (SA) modified BaSO4 nanofillers were used to examine the effect of functionalization. Rigid nanofillers improved the tensile modulus and strength of PLLA (60% and 110% respectively), while the use of SA-BaSO4 caused a significant increase (~110%) in the elongation at break. Enhancement in mechanical properties is attributed to functionalization which decreased the agglomeration of the nanofillers and improved dispersion. The nanocomposites were also radiopaque. Finite element analysis (FEA) showed that scaffold fabricated from the novel nanocomposite material has improved scaffolding ability, specifically that the strut thickness could be decreased compared to the conventional PLLA scaffold. In conclusion, BaSO4/PLLA-based nanocomposites could potentially be used as materials for BRS with improved mechanical and radiopaque properties.

show abstract

Ionic liquid-functionalized crystals of barium sulfate: A hybrid organic–inorganic material with tuned hydrophilicity and solid–liquid behavior

Cited by 8 publications

References 26 publications

Ionic-Liquid-Functionalized Mineral Particles for Protein Crystallization

Ionic-Liquid-Functionalized Mineral Particles for Protein Crystallization

Effect of Infrared Light on Protein Behavior in Contact with Solid Surface

Radiopaque Fully Degradable Nanocomposites for Coronary Stents

Contact Info

Product

Resources

About