The fate of a designed protein corona on nanoparticles in vitro and in vivo

• Denise Bargheer,
• Julius Nielsen,
• Gabriella Gébel,
• Markus Heine,
• Sunhild C. Salmen,
• Roland Stauber,
• Horst Weller,
• Joerg Heeren and
• Peter Nielsen

Beilstein J. Nanotechnol. 2015, 6, 36–46, doi:10.3762/bjnano.6.5

• surface was modified by PEGylation with mono- or bifunctional poly(ethylene oxide)amines (PEG). Using 125I-labeled test proteins (transferrin, albumin), the binding and exchange of corona proteins was studied first in vitro. Incubation with 125I-transferrin showed that with increasing grade of PEGylation

• the binding was substantially diminished without a difference between simply adsorbed and covalently bound protein. However, after incubation with excess albumin and subsequently whole plasma, transferrin from the preformed transferrin corona was more and more lost from SPIOs in the case of adsorbed

• proteins. If non-labeled transferrin was used as preformed corona and excess 125I-labeled albumin was added to the reaction mixtures with different SPIOs, a substantial amount of label was bound to the particles with initially adsorbed transferrin but little or even zero with covalently bound transferrin

Proinflammatory and cytotoxic response to nanoparticles in precision-cut lung slices

• Stephanie Hirn,
• Nadine Haberl,
• Kateryna Loza,
• Matthias Epple,
• Wolfgang G. Kreyling,
• Barbara Rothen-Rutishauser,
• Markus Rehberg and
• Fritz Krombach

Beilstein J. Nanotechnol. 2014, 5, 2440–2449, doi:10.3762/bjnano.5.253

• nucleoside analogue to thymidine) at 0, 20, 44, and 68 h after preparation. Subsequently, four PCLS per time point were fixed with buffered 4% paraformaldehyde (Microcos GmbH, Saaldorf-Surheim, Germany) at room temperature for 15 min. Then PCLS were washed twice in PBS supplemented with 3% bovine albumin

Inorganic Janus particles for biomedical applications

• Isabel Schick,
• Steffen Lorenz,
• Dominik Gehrig,
• Stefan Tenzer,
• Wiebke Storck,
• Karl Fischer,
• Dennis Strand,
• Frédéric Laquai and
• Wolfgang Tremel

Beilstein J. Nanotechnol. 2014, 5, 2346–2362, doi:10.3762/bjnano.5.244

• binding of apolipoproteins and serum albumin to hydrophobic nanoparticles by Cedervall and co-workers [115]. Interestingly, there is a significant and unexpected difference in the composition of the protein corona of isotropic silica encapsulated MnO and Fe3O4 nanoparticles. By studying the protein

Coating with luminal gut-constituents alters adherence of nanoparticles to intestinal epithelial cells

• Heike Sinnecker,
• Katrin Ramaker and
• Andreas Frey

Beilstein J. Nanotechnol. 2014, 5, 2308–2315, doi:10.3762/bjnano.5.239

• the presence of the proteins bovine serum albumin (BSA) and casein the fluorescence intensities were discernibly decreased, no matter of which size the NPs were. We speculate that a protein coating produced by passive adsorption of the proteins to the NPs is responsible for this observed reduction in

• ], and possible implications for the particle–cell interactions are considered. For example, it was shown that human serum albumin (HSA), BSA and fetal bovine serum can build a protein corona around NPs whereby the particles are stabilized against agglomeration and the colloid stability of the particle

Anticancer efficacy of a supramolecular complex of a 2-diethylaminoethyl–dextran–MMA graft copolymer and paclitaxel used as an artificial enzyme

• Yasuhiko Onishi,
• Yuki Eshita,
• Rui-Cheng Ji,
• Masayasu Onishi,
• Takashi Kobayashi,
• Masaaki Mizuno,
• Jun Yoshida and
• Naoji Kubota

Beilstein J. Nanotechnol. 2014, 5, 2293–2307, doi:10.3762/bjnano.5.238

• polyglutamate [43] and albumin [44], encapsulated in cationic liposomes [45], or PEG-polyaspartate [46]. By using these carriers, PTX is thought to be transported into and released directly in cells, thus improving its efficacy. However, the DDMC/PTX complex will be not degraded in the cell, and its efficacy

Nanoencapsulation of ultra-small superparamagnetic particles of iron oxide into human serum albumin nanoparticles

• Matthias G. Wacker,
• Mahmut Altinok,
• Stephan Urfels and
• Johann Bauer

Beilstein J. Nanotechnol. 2014, 5, 2259–2266, doi:10.3762/bjnano.5.235

• Technische Universität Darmstadt, Technical Chemistry, D-64287 Darmstadt, Germany Merck KGaA, D-64287 Darmstadt, Germany 10.3762/bjnano.5.235 Abstract Human serum albumin nanoparticles have been utilized as drug delivery systems for a variety of medical applications. Since ultra-small superparamagnetic

• with the surface modification and nanoencapsulation of USPIO into an albumin matrix by using ethanolic desolvation. Particles of narrow size distribution and with a defined particle structure have been achieved. Keywords: diagnostics; HSA; nanoencapsulation; nanoparticles; USPIO; Introduction Over

• systemic exposition of patients with the carrier [6]. Human serum albumin (HSA) represents a promising candidate that binds a wide range of compounds with different physicochemical characteristics. In 2007, with Abraxane®, a first polymeric nanoparticle formulation consisting of this material has been

Biopolymer colloids for controlling and templating inorganic synthesis

• Laura C. Preiss,
• Katharina Landfester and
• Rafael Muñoz-Espí

Beilstein J. Nanotechnol. 2014, 5, 2129–2138, doi:10.3762/bjnano.5.222

• synthetic polymers (see Section 4 in [60] for a review), but only a limited number of works are found for biopolymers. Li et al. [61] prepared cross-linked chitosan microspheres and immobilized bovine serum albumin covalently on their surface. On the resulting particles, silica was formed by a sol–gel

Effects of surface functionalization on the adsorption of human serum albumin onto nanoparticles – a fluorescence correlation spectroscopy study

• Pauline Maffre,
• Stefan Brandholt,
• Karin Nienhaus,
• Li Shang,
• Wolfgang J. Parak and
• G. Ulrich Nienhaus

Beilstein J. Nanotechnol. 2014, 5, 2036–2047, doi:10.3762/bjnano.5.212

• Marburg, Renthof 7, 35037 Marburg, Germany, Department of Physics, University of Illinois at Urbana-Champaign, 1110 West Green Street, Urbana, IL 61801, USA 10.3762/bjnano.5.212 Abstract By using fluorescence correlation spectroscopy (FCS), we have studied the adsorption of human serum albumin (HSA) onto

• four orders of magnitude. These variations can be understood in terms of specific Coulombic interactions between the proteins and the NP surfaces. Keywords: fluorescence correlation spectroscopy; human serum albumin; nanoparticles; protein corona; quantum dots; Introduction In recent years, both

• reliable in our hands. In our original FCS study [45], we investigated the adsorption of human serum albumin (HSA) onto carboxyl-functionalized, polymer-encased iron platinum nanoparticles (Fe–Pt NPs) with a hydrodynamic radius, RH, of 5–6 nm. We prepared HSA solutions of different concentrations in

PVP-coated, negatively charged silver nanoparticles: A multi-center study of their physicochemical characteristics, cell culture and in vivo experiments

• Sebastian Ahlberg,
• Alexandra Antonopulos,
• Jörg Diendorf,
• Ralf Dringen,
• Matthias Epple,
• Rebekka Flöck,
• Wolfgang Goedecke,
• Christina Graf,
• Nadine Haberl,
• Jens Helmlinger,
• Fabian Herzog,
• Frederike Heuer,
• Stephanie Hirn,
• Christian Johannes,
• Stefanie Kittler,
• Manfred Köller,
• Katrin Korn,
• Wolfgang G. Kreyling,
• Fritz Krombach,
• Jürgen Lademann,
• Kateryna Loza,
• Eva M. Luther,
• Marcelina Malissek,
• Martina C. Meinke,
• Daniel Nordmeyer,
• Anne Pailliart,
• Jörg Raabe,
• Fiorenza Rancan,
• Barbara Rothen-Rutishauser,
• Eckart Rühl,
• Carsten Schleh,
• Andreas Seibel,
• Christina Sengstock,
• Lennart Treuel,
• Annika Vogt,
• Katrin Weber and
• Reinhard Zellner

Beilstein J. Nanotechnol. 2014, 5, 1944–1965, doi:10.3762/bjnano.5.205

• adsorption onto nanoparticle surfaces is a critical step towards understanding the formation of the protein corona at the full complexity of the physiological situation [45][54][55][56][57][58]. We have investigated the formation of a protein corona of serum albumin around silver nanoparticles [56

• ]. Specifically, we have addressed the effect of a PVP coating around the metallic surface of silver and, for comparison, gold nanoparticles, on the adsorption/desorption equilibrium of serum albumin molecules – an established model protein [57][59][60][61][62]. To quantify this equilibrium, we have used circular

• ][68], the quantitative analysis of the corresponding CD signals has been shown to be a good indicator for the overall extent to which the original secondary structure of serum albumin is preserved in the "equilibrated" corona [54][69][70]. The exact mechanisms of partial or full protein denaturation

Imaging the intracellular degradation of biodegradable polymer nanoparticles

• Anne-Kathrin Barthel,
• Martin Dass,
• Melanie Dröge,
• Jens-Michael Cramer,
• Daniela Baumann,
• Markus Urban,
• Katharina Landfester,
• Volker Mailänder and
• Ingo Lieberwirth

Beilstein J. Nanotechnol. 2014, 5, 1905–1917, doi:10.3762/bjnano.5.201

• bovine serum albumin (BSA), which is a main component of FCS that is added to the cell medium. The results showed that BSA significantly increased the exocytosis of the tested PLGA nanoparticles [28]. Given that we used FCS in the cell medium, the high exocytosis might be responsible for the significant

Biocompatibility of cerium dioxide and silicon dioxide nanoparticles with endothelial cells

• Claudia Strobel,
• Martin Förster and
• Ingrid Hilger

Beilstein J. Nanotechnol. 2014, 5, 1795–1807, doi:10.3762/bjnano.5.190

• with buffer (1% BSA [Albumin Fraktion V, Carl Roth GmbH & CO. KG, Germany] in Hank’s BSS [PAA Laboratories GmbH, Austria]). Then the cells were fixed with 2% (v/v) formaldehyde (Carl Roth GmbH & CO. KG, Germany) in Hank’s BSS for 15 min at room temperature. The cells were then washed with Hank’s BSS

In vitro and in vivo interactions of selected nanoparticles with rodent serum proteins and their consequences in biokinetics

• Wolfgang G. Kreyling,
• Stefanie Fertsch-Gapp,
• Martin Schäffler,
• Blair D. Johnston,
• Nadine Haberl,
• Christian Pfeiffer,
• Jörg Diendorf,
• Carsten Schleh,
• Stephanie Hirn,
• Manuela Semmler-Behnke,
• Matthias Epple and
• Wolfgang J. Parak

Beilstein J. Nanotechnol. 2014, 5, 1699–1711, doi:10.3762/bjnano.5.180

• agglomeration behavior [5]. The proteins chosen were albumin, transferrin and apolipoprotein A-1, which exist both in blood serum and in the lung epithelial lining fluid. Protein concentrations before and after NP incubation were determined by a depletion method using the Bio-Rad protein assay. In all cases, a

• protein in the circulation), serum albumin (most abundant blood multi-functional protein), fibrinogen beta (modulation of blood coagulation and opsonisation of foreign bodies [8]), and apolipoprotein E (ApoE) (mediating protein for transcytosis across biological membranes [9][10]). More detected proteins

• groups, but also with polyethylene glycol (PEG) or other polymers or polyelectrolytes and, finally, with tightly grafted plasma proteins (albumin or apolipoprotein E). All AuNP had been radioactively labeled with 198Au by neutron activation in a nuclear research reactor. Most of these studies were

Current state of laser synthesis of metal and alloy nanoparticles as ligand-free reference materials for nano-toxicological assays

• Christoph Rehbock,
• Jurij Jakobi,
• Lisa Gamrad,
• Selina van der Meer,
• Daniela Tiedemann,
• Ulrike Taylor,
• Wilfried Kues,
• Detlef Rath and
• Stephan Barcikowski

Beilstein J. Nanotechnol. 2014, 5, 1523–1541, doi:10.3762/bjnano.5.165

• , mammalian cells and bacteria are considered. Keywords: albumin; gold-silver; implant alloy; laser ablation; nickel-titanium; size control; wear debris; Introduction The widespread use of medical implants consisting of metals (e.g., gold coatings [1]) and alloys (e.g., NiTi, CoCr, stainless steel) [2][3][4

• ). In this case quenching of particle growth was achieved by albumin addition at a fixed position in a flow-through reactor (reactor design described elsewhere [81]) (Figure 4C, black curve). Here, particle diameters were determined by analytical disk centrifugation and size control in a regime of 15–34

• occur on bare nanoparticle surfaces [111]. In order to examine the influence of protein stabilization on ligand-free nanoparticles, albumin may be an appropriate model substance, which is known to be abundant in the protein corona and is one of the most frequent proteins in serum-containing cell culture

In vitro interaction of colloidal nanoparticles with mammalian cells: What have we learned thus far?

• Moritz Nazarenus,
• Qian Zhang,
• Mahmoud G. Soliman,
• Pablo del Pino,
• Beatriz Pelaz,
• Susana Carregal-Romero,
• Joanna Rejman,
• Barbara Rothen-Rutishauser,
• Martin J. D. Clift,
• Reinhard Zellner,
• G. Ulrich Nienhaus,
• James B. Delehanty,
• Igor L. Medintz and
• Wolfgang J. Parak

Beilstein J. Nanotechnol. 2014, 5, 1477–1490, doi:10.3762/bjnano.5.161

• metal NPs, in particular to Au NPs [125][126]. v) Proteins, in general, tend to adsorb to surfaces, which is also true on the nanometer scale. Adsorption of albumin is, for example, an integral part of opsonization [127][128]. The proteins adsorbed to the surface of NPs are typically termed protein

• fluorescence correlation spectroscopy (FCS), Röcker et al. investigated the adsorption of human serum albumin onto FePt NPs and found clear evidence that the proteins formed a monolayer on the surface of the NP [136]. Additional FCS studies by using other important serum proteins invariably confirmed the

Protein-coated pH-responsive gold nanoparticles: Microwave-assisted synthesis and surface charge-dependent anticancer activity

• Dickson Joseph,
• Nisha Tyagi,
• Christian Geckeler and
• Kurt E.Geckeler

Beilstein J. Nanotechnol. 2014, 5, 1452–1462, doi:10.3762/bjnano.5.158

• ]. Biomolecules have been reported to interact with gold salts and reduce them into metallic gold, acting both as a reductant and stabilizer [12][17][18][19][20][21]. Proteins, such as bovine serum albumin, silk fibroin protein, chicken egg white lysozyme, α-amylase, green fluorescent protein and apoferritin have

• mg/mL and 0.5 mM, respectively. These conditions did not result in the formation of AuNPs. The addition of Ag ions to a mixture containing Au ions has been reported to form AuNPs in the presence of bovine serum albumin (BSA) [33]. Hence, we added AgNO3 at a ratio of 5:1 between the Au and Ag ions and

• histone (HIS), chicken egg white lysozyme (LYS), ovalbumin (OVA), bovine serum albumin (BSA), bovine hemoglobin (BHG), bovine gamma globulin (BGG), glucose oxidase (Aspergillus niger) (GOX), and trypsin (porcine pancreas, TRY), used for the experiments were obtained from Sigma (USA) as a lyophilized

The protein corona protects against size- and dose-dependent toxicity of amorphous silica nanoparticles

• Dominic Docter,
• Christoph Bantz,
• Dana Westmeier,
• Hajo J. Galla,
• Qiangbin Wang,
• James C. Kirkpatrick,
• Peter Nielsen,
• Michael Maskos and
• Roland H. Stauber

Beilstein J. Nanotechnol. 2014, 5, 1380–1392, doi:10.3762/bjnano.5.151

• albumin, indicated by the prominent protein band of approximately 70 kDa, high molecular weight proteins were found to be enriched particularly on the ASP30 and ASP30L. Discussion Besides ingestion, inhalation is one of the major entry routes for nanomaterials into the GI tract. Indeed, the majority of

Nanodiamond-DGEA peptide conjugates for enhanced delivery of doxorubicin to prostate cancer

• Amanee D Salaam,
• Patrick Hwang,
• Roberus McIntosh,
• Hadiyah N Green,
• Ho-Wook Jun and
• Derrick Dean

Beilstein J. Nanotechnol. 2014, 5, 937–945, doi:10.3762/bjnano.5.107

• tumor types [6][7][8][9]. Currently, there are several clinically approved nanoparticle-based cancer drugs using liposomes, nanoparticle albumin-bound (nab) technology, dendrimers, polymeric, carbon, and metal nanoparticles [6][8]. Gold nanorods, iron magnetic nanoparticles, polymer nanospheres, lipids

Antimicrobial nanospheres thin coatings prepared by advanced pulsed laser technique

• Alina Maria Holban,
• Valentina Grumezescu,
• Alexandru Mihai Grumezescu,
• Bogdan Ştefan Vasile,
• Roxana Truşcă,
• Rodica Cristescu,
• Gabriel Socol and
• Florin Iordache

Beilstein J. Nanotechnol. 2014, 5, 872–880, doi:10.3762/bjnano.5.99

• polymeric microspheres. Thus, Socol et al., [43], firstly reported the novel deposition of PLGA–PVA, PLGA–PVA–BSA (bovine serum albumin) and PLGA–PVA–CS microspheres by matrix assisted pulsed laser evaporation (MAPLE) technique. SEM images of thin coatings reveal homogeneous and spherical-shaped particles

• in the micrometric range. The average diameter of PLGA–PVA, PLGA–PVA–BSA (bovine serum albumin) and PLGA–PVA–CS particles ranged from 180 to 250 nm. Grumezescu et al., [34], reported the MAPLE fabrication of PLA–PVA–UA microsphere thin coatings. These thin coatings possessed a homogeneous shape and

One pot synthesis of silver nanoparticles using a cyclodextrin containing polymer as reductant and stabilizer

• Arkadius Maciollek and
• Helmut Ritter

Beilstein J. Nanotechnol. 2014, 5, 380–385, doi:10.3762/bjnano.5.44

• mL/min. The molecular weight was calculated with Astra5 software from static light scattering data, using Zimm-model. As concentration source, the refractive index was used. Calibration of the system was performed with bovin serum albumin. The absorption spectra were measured on a Specord 210 Plus UV

Modulation of defect-mediated energy transfer from ZnO nanoparticles for the photocatalytic degradation of bilirubin

• Tanujjal Bora,
• Karthik K. Lakshman,
• Soumik Sarkar,
• Abhinandan Makhal,
• Samim Sardar,
• Samir K. Pal and
• Joydeep Dutta

Beilstein J. Nanotechnol. 2013, 4, 714–725, doi:10.3762/bjnano.4.81

• [1] and can exist in the body both as a free molecule and as an albumin complex. The unconjugated (Z,Z)-BR isomer is insoluble in water and is converted in the liver into the water-soluble (Z,E)-BR isomer with the assistance of glucuronic acid. Most of the BR is then extracted in the bile while a

• molecules on ZnO nanostructures, a resonant defect-mediated energy transfer from the photo-excited ZnO nanostructures to the BR molecules induces their photodegradation [15]. It was also demonstrated that the system can effectively degrade BR when it is bound to albumin. Although literature related to the

Porous polymer coatings as substrates for the formation of high-fidelity micropatterns by quill-like pens

• Michael Hirtz,
• Marcus Lyon,
• Wenqian Feng,
• Andrea E. Holmes,
• Harald Fuchs and
• Pavel A. Levkin

Beilstein J. Nanotechnol. 2013, 4, 377–384, doi:10.3762/bjnano.4.44

• micrometres. The bromophenol blue arrays on HEMA support were used to detect the presence of bovine serum albumin (BSA). In the presence of BSA, the fluorescence spectrum observed from the bromophenol blue microarray exhibited a significant red shift of the maximum emission wavelength. Our results show that

• samples [12][13]. After preparing 10 × 10 spot microarrays using bromophenol blue solution as shown in the inset of Figure 6b, the patterns were either incubated with a 0.5 µL droplet of an analyte solution containing bovine serum albumin (BSA) or a clear solution to give a negative control. Fluorescence

Macromolecular shape and interactions in layer-by-layer assemblies within cylindrical nanopores

• Thomas D. Lazzara,
• K. H. Aaron Lau,
• Wolfgang Knoll,
• Andreas Janshoff and
• Claudia Steinem

Beilstein J. Nanotechnol. 2012, 3, 475–484, doi:10.3762/bjnano.3.54

• serum albumin was compared with that of linear polyelectrolytes (linear-PEs), both species being of similar molecular weight. LbL deposition within the cylindrical AAO geometry for different pore diameters (d0 = 25–80 nm) for the various macromolecular species, showed that the multilayer film growth was

• molecular recognition of biotinylated-bovine serum albumin (b-BSA) by avidin. Avidin has four biotin-binding sites, whereas the b-BSA used has 13 biotin molecules per protein on average. Avidin with a mass of MW = 66–69 kDa, and which is positively charged at neutral pH, was first adsorbed onto the

• Calbiochem (purity 12.9 units/mg). Biotinylated-bovine serum albumin (b-BSA) with 13 mol biotin/mol albumin, poly(sodium 4-styrenesulfonate) (PSS) (Mw = 70 kDa), poly(allylamine hydrochloride) PAH (Mw = 50–65 kDa), CuCl2, NaCl, and 16-mercaptohexadecanoic acid (90%) were purchased from Sigma Aldrich (St

Analysis of fluid flow around a beating artificial cilium

• Mojca Vilfan,
• Gašper Kokot,
• Andrej Vilfan,
• Natan Osterman,
• Blaž Kavčič,
• Igor Poberaj and
• Dušan Babič

Beilstein J. Nanotechnol. 2012, 3, 163–171, doi:10.3762/bjnano.3.16

• diameter 55 nm [24]) in water. To prevent aggregation of the beads, we coated them with BSA (bovine serum albumin), 10 mg/mL, for 4 h in an ultrasonic bath. One end of the assembled chain was attached to the surface through prefabricated ferromagnetic-nickel anchoring sites. The nickel dots were

Characterization of protein adsorption onto FePt nanoparticles using dual-focus fluorescence correlation spectroscopy

• Pauline Maffre,
• Karin Nienhaus,
• Faheem Amin,
• Wolfgang J. Parak and
• G. Ulrich Nienhaus

Beilstein J. Nanotechnol. 2011, 2, 374–383, doi:10.3762/bjnano.2.43

• , namely serum albumin, apolipoprotein A-I and apolipoprotein E4, onto polymer-coated, fluorescently labeled FePt nanoparticles (~12 nm diameter) carrying negatively charged carboxyl groups on their surface. For all three proteins, a step-wise increase in hydrodynamic radius with protein concentration was

• correlation spectroscopy; human serum albumin; nanoparticle; protein adsorption; Introduction Recent years have seen enormous advances in the field of nanotechnology. A huge variety of nanoparticles (NPs), defined as objects with all three spatial dimensions in the range of 1–100 nm, has been developed, with

• understand the structural and dynamic properties of the protein corona at the molecular level. Recently, we have used quantitative fluorescence microscopy, especially fluorescence correlation spectroscopy (FCS), to study protein adsorption of human serum albumin (HSA) on polymer-coated FePt NPs with an

Magnetic nanoparticles for biomedical NMR-based diagnostics

• Huilin Shao,
• Tae-Jong Yoon,
• Monty Liong,
• Ralph Weissleder and
• Hakho Lee

Beilstein J. Nanotechnol. 2010, 1, 142–154, doi:10.3762/bjnano.1.17

• bovine serum albumin (BSA) protein as a control did not elicit any change in T2 (Figure 5b). More recently, MRSw biosensors, capable of detecting soluble tumor biomarker proteins (such as CA-125, VEGF, and α-fetoprotein) were described, and used for parallel detection of multiple markers in blood samples