Bovine Serum Albumin Adsorption onto Colloidal Al<sub>2</sub>O<sub>3</sub> Particles:  A New Model Based on Zeta Potential and UV−Vis Measurements

Rezwan, Kurosch; Meier, Lorenz; Rezwan, Mandana; Vörös, János; Textor, Marcus; Gauckler, Ludwig J.

doi:10.1021/la048459k

Cited by 296 publications

(281 citation statements)

References 47 publications

(73 reference statements)

Supporting

Mentioning

243

Contrasting

Unclassified

Order By: Relevance

“…Close to the pI, the electrostatic interaction is weak, and the protein will likely be randomly oriented at the NP surface, whereas at pH 7.5, protein orientation is dictated by charge density matching between oppositely charged domains. BSA does not undergo any significant conformational changes in the pH range from pH 4 to pH 8 [35], which reinforces the hypothesis of the initial interaction between PBCA NPs and BSA being predominantly electrostatic in nature [36].…”

Section: Np-stabilized Mbssupporting

confidence: 84%

Nanoparticle‐stabilized microbubbles for multimodal imaging and drug delivery

Mørch

Hansen

Berg

et al. 2015

Contrast Media & Molecular

View full text Add to dashboard Cite

Microbubbles (MBs) are routinely used as contrast agents for ultrasound imaging. The use of ultrasound in combination with MBs has also attracted attention as a method to enhance drug delivery.We have developed a technology platform incorporating multiple functionalities, including imaging and therapy in a single system consisting of MBs stabilized by polyethylene glycol (PEG) coated polymeric nanoparticles (NPs). The NPs, containing lipophilic drugs and/or contrast agents, are composed of the widely used poly(butyl cyanoacrylate) (PBCA) polymer and prepared in a single step. MBs stabilized by these NPs are subsequently prepared by self-assembly of NPs at the MB air/liquid interface. Here we show that these MBs can act as contrast agents for conventional ultrasound imaging. Successful encapsulation of iron oxide NPs inside the PBCA NPs is demonstrated, potentially enabling the NPs/MBs to be used as magnetic resonance imaging (MRI) and/or molecular ultrasound imaging contrast agents. By precise tuning of the applied ultrasound pulse, the MBs burst and the NPs constituting the shell are released. This could result in increased local deposit of NPs into target tissue providing improved therapy and imaging contrast compared to freely distributed NPs.

show abstract

Section: Np-stabilized Mbssupporting

confidence: 84%

Nanoparticle‐stabilized microbubbles for multimodal imaging and drug delivery

Mørch

Hansen

Berg

et al. 2015

Contrast Media & Molecular

View full text Add to dashboard Cite

show abstract

“…Within the assumption of coinciding center of mass positions of the S distribution and of the whole protein, this indicates that the fully hydrated protein layer is as thick as d HSA ∼ 2Δz = 2z S ∼ 60-80 Å. For the width of the S distribution, we consistently obtain σ S = 20 ± 5 Å, corresponding to an FWHM = 48 ± 12 Å. Adsorption of serum albumin to Al oxide has been previously investigated using zeta-potential and UVVis measurements, and a layer thickness of about 55 Å under water was reported and interpreted as side-on configuration (31). Thicker serum albumin layers of more than 100 Å and up to 70 Å were reported for mica/water (36) and air/water interfaces (37), respectively.…”

Section: Resultssupporting

confidence: 55%

Atom-scale depth localization of biologically important chemical elements in molecular layers

Schneck

Scoppola

Drnec

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

In nature, biomolecules are often organized as functional thin layers in interfacial architectures, the most prominent examples being biological membranes. Biomolecular layers play also important roles in context with biotechnological surfaces, for instance, when they are the result of adsorption processes. For the understanding of many biological or biotechnologically relevant phenomena, detailed structural insight into the involved biomolecular layers is required. Here, we use standing-wave X-ray fluorescence (SWXF) to localize chemical elements in solid-supported lipid and protein layers with near-Ångstrom precision. The technique complements traditional specular reflectometry experiments that merely yield the layers' global density profiles. While earlier work mostly focused on relatively heavy elements, typically metal ions, we show that it is also possible to determine the position of the comparatively light elements S and P, which are found in the most abundant classes of biomolecules and are therefore particularly important. With that, we overcome the need of artificial heavy atom labels, the main obstacle to a broader application of high-resolution SWXF in the fields of biology and soft matter. This work may thus constitute the basis for the label-free, element-specific structural investigation of complex biomolecular layers and biological surfaces.surfaces | interfaces | lipid membranes | protein adsorption | X-ray scattering N anometric biomolecular layers in interfacial geometries are key components of biological matter. Biological membranes, for example, are 2D molecular structures composed mainly of lipids and proteins in an aqueous environment (1, 2). Interfacial biomolecular layers are also important from a biotechnological perspective, where surfaces are often designed to selectively promote or prevent the adsorption of bio(macro)molecules from solution (3). To investigate the diverse behavior of biomolecules at interfaces, well-defined planar model systems of biological and biotechnologically relevant interfaces have been established (4, 5). Processes involving biomolecules at interfaces are typically accompanied by a spatial reorganization of molecules, changes in molecular conformations, or the adsorption of molecules in a chemically heterogeneous environment (6). Structural insight on the nanometer scale is therefore of paramount importance.X-ray and neutron scattering are uniquely suited for the structural investigation of biomolecular systems. Specular reflectometry reveals matter density profiles perpendicular to a planar interface. However, it is generally difficult to elucidate molecular conformations and elemental distributions from such "global" density profiles. In contrast, standing-wave X-ray fluorescence (SWXF) allows determining element-specific density profiles across an interface. The SWXF technique is based on the elementcharacteristic fluorescence induced by a standing X-ray wave. The latter is formed by interference of the incident and reflected waves and its shape depends o...

show abstract

“…Furthermore, the accuracy of the UV-vis spectrometer of 2 milli absorbance limits the resolution of the recorded wavelength shifts. Compared with a protein with similar size like bovine serum albumin (BSA; 5.5 Â 5.5 Â 9 nm) 41 it is reported that 3.7 ( ± 0.2) Â 1,012 molecules bind per cm 2.42. This implies that B12 BSA molecules can bind to the surface of a 10-nm AuNP by an end-on mechanism.…”

Section: Resultsmentioning

confidence: 99%

Molecular protein adaptor with genetically encoded interaction sites guiding the hierarchical assembly of plasmonically active nanoparticle architectures

et al. 2015

View full text Add to dashboard Cite

The control over the defined assembly of nano-objects with nm-precision is important to create systems and materials with enhanced properties, for example, metamaterials. In nature, the precise assembly of inorganic nano-objects with unique features, for example, magnetosomes, is accomplished by efficient and reliable recognition schemes involving protein effectors. Here we present a molecular approach using protein-based 'adaptors/ connectors' with genetically encoded interaction sites to guide the assembly and functionality of different plasmonically active gold nanoparticle architectures (AuNP). The interaction of the defined geometricaly shaped protein adaptors with the AuNP induces the self-assembly of nanoarchitectures ranging from AuNP encapsulation to one-dimensional chain-like structures, complex networks and stars. Synthetic biology and bionanotechnology are applied to co-translationally encode unnatural amino acids as additional site-specific modification sites to generate functionalized biohybrid nanoarchitectures. This protein adaptor-based nanoobject assembly approach might be expanded to other inorganic nano-objects creating biohybrid materials with unique electronic, photonic, plasmonic and magnetic properties.

show abstract

Bovine Serum Albumin Adsorption onto Colloidal Al₂O₃ Particles: A New Model Based on Zeta Potential and UV−Vis Measurements

Cited by 296 publications

References 47 publications

Nanoparticle‐stabilized microbubbles for multimodal imaging and drug delivery

Nanoparticle‐stabilized microbubbles for multimodal imaging and drug delivery

Atom-scale depth localization of biologically important chemical elements in molecular layers

Molecular protein adaptor with genetically encoded interaction sites guiding the hierarchical assembly of plasmonically active nanoparticle architectures

Contact Info

Product

Resources

About

Bovine Serum Albumin Adsorption onto Colloidal Al2O3 Particles: A New Model Based on Zeta Potential and UV−Vis Measurements

Cited by 296 publications

References 47 publications

Nanoparticle‐stabilized microbubbles for multimodal imaging and drug delivery

Nanoparticle‐stabilized microbubbles for multimodal imaging and drug delivery

Atom-scale depth localization of biologically important chemical elements in molecular layers

Molecular protein adaptor with genetically encoded interaction sites guiding the hierarchical assembly of plasmonically active nanoparticle architectures

Contact Info

Product

Resources

About

Bovine Serum Albumin Adsorption onto Colloidal Al₂O₃ Particles: A New Model Based on Zeta Potential and UV−Vis Measurements