Uptake of the proteins HTRA1 and HTRA2 by cells mediated by calcium phosphate nanoparticles

• Olga Rotan,
• Katharina N. Severin,
• Simon Pöpsel,
• Alexander Peetsch,
• Melisa Merdanovic,
• Michael Ehrmann and
• Matthias Epple

Beilstein J. Nanotechnol. 2017, 8, 381–393, doi:10.3762/bjnano.8.40

• denoted as HTRA1-488 and HTRA2-488 in the following. Fluorescein-isothiocyanate (FITC)-labelled bovine serum albumin (denoted as BSA-FITC in the following) was obtained from Sigma-Aldrich (Germany). Synthesis of the protein-loaded calcium phosphate nanoparticles The nanoparticles were synthesized as

Comparison of four methods for the biofunctionalization of gold nanorods by the introduction of sulfhydryl groups to antibodies

• Xuefeng Wang,
• Zhong Mei,
• Yanyan Wang and
• Liang Tang

Beilstein J. Nanotechnol. 2017, 8, 372–380, doi:10.3762/bjnano.8.39

• modification with Traut’s reagent. These results are consistent with the findings that DTT modification introduces more sulfhydryl groups per mol human serum albumin (HSA) than treatment with Traut’s reagent [28]. The conjugating efficiency of antibody-to-nanosphere by Traut’s thiolation was low relative to

Comparison of four functionalization methods of gold nanoparticles for enhancing the enzyme-linked immunosorbent assay (ELISA)

• Paula Ciaurriz,
• Fátima Fernández,
• Edurne Tellechea,
• Jose F. Moran and
• Aaron C. Asensio

Beilstein J. Nanotechnol. 2017, 8, 244–253, doi:10.3762/bjnano.8.27

• serum albumin (BSA) were added and shaken for 10 min. Thereafter the sample was centrifuged (7,500g 30 min) to remove unbound protein and AuNPs were re-suspended in 1 mL of 2 mM borate buffer pH 8.7 containing 5% sucrose, 2% glycerol, 0.5% BSA, and 0.01% Tween. The washing step was repeated once and the

Performance of colloidal CdS sensitized solar cells with ZnO nanorods/nanoparticles

• Anurag Roy,
• Partha Pratim Das,
• Mukta Tathavadekar,
• Sumita Das and
• Parukuttyamma Sujatha Devi

Beilstein J. Nanotechnol. 2017, 8, 210–221, doi:10.3762/bjnano.8.23

• Division, CSIR-National Chemical Laboratory, Pune 411 008, India 10.3762/bjnano.8.23 Abstract As an alternative photosensitizer in dye-sensitized solar cells, bovine serum albumin (BSA) (a nonhazardous protein) was used in the synthesis of colloidal CdS nanoparticles (NPs). This system has been employed

• dots (QDs) we followed a bioinspired strategy to synthesize such systems. In this work, bovine serum albumin (BSA) is selected as a biotemplating agent. BSA is a ubiquitous protein mainly present in blood and is a commonly used reagent in biological studies. Here, we have synthesized functionalized

• and ethanol were purchased from Merck Limited, Germany. Bovine serum albumin was purchased from Sigma-Aldrich, USA. Zn(NO3)3 and Zn(CH3COO)2 were purchased from Merck Limited, Germany. All the chemicals were used without any further purification. Synthesis of CdS nanoparticles The CdS NPs were

Structural and tribometric characterization of biomimetically inspired synthetic "insect adhesives"

• Matthias W. Speidel,
• Malte Kleemeier,
• Andreas Hartwig,
• Klaus Rischka,
• Angelika Ellermann,
• Rolf Daniels and
• Oliver Betz

Beilstein J. Nanotechnol. 2017, 8, 45–63, doi:10.3762/bjnano.8.6

• adhesivenesses, ranging between 1–18 mN. The adhesive performance was drastically reduced in the emulsions that contained albumin as the protein component or that lacked protein. Tribometric shear tests were performed at moderate normal loads. Our measured friction forces (4–93 mN in the first and 0.1–5.8 mN in

• (C30) representing hydrocarbons of defined structure and length within the range of C23–C49 as established in the biological role models. Albumin and gelatin were substitutes for proteinogenic amino acids, with the surfactant Span 80 (Sorbitane monooleate) being used as a combined replacement for fatty

• up to 60 s−1. For this analysis, we examined the emulsions consisting of squalane and the proteins gelatin and albumin, respectively. We propose that a yield point is required for a locomotion adhesive to prevent the sliding of a non-moving insect from a vertical smooth surface. Therefore, the

Effective intercalation of zein into Na-montmorillonite: role of the protein components and use of the developed biointerfaces

• Ana C. S. Alcântara,
• Margarita Darder,
• Pilar Aranda and
• Eduardo Ruiz-Hitzky

Beilstein J. Nanotechnol. 2016, 7, 1772–1782, doi:10.3762/bjnano.7.170

• intercalation of gelatin into montmorillonite [4], other biohybrids also based on the assembly of smectite clays and proteins (e.g., bovine serum albumin, gelatin, casein or soy) have been vastly studied [5][6][7][8][9][10]. However, protein adsorption on montmorillonite clay can be considered a complex process

• proteins intercalated in sodium montmorillonite, such as bovine serum albumin (BSA) [5]. Therefore, the new route 2 seems more effective to achieve the incorporation of zein molecules into the intracrystalline space of sodium montmorillonite. The infrared spectra of pristine MMT, zein, and Z-MMT_S2

• biohybrid (1.88 nm), which is the biohybrid prepared by synthesis 2 route using the highest amount of zein (Figure 2b). These results are in agreement with those reported by Weiss [11], which revealed that intercalation of several proteins, such as salmin, serum and egg albumin, generally never surpasses a

High performance Ce-doped ZnO nanorods for sunlight-driven photocatalysis

• Bilel Chouchene,
• Tahar Ben Chaabane,
• Lavinia Balan,
• Emilien Girot,
• Kevin Mozet,
• Ghouti Medjahdi and
• Raphaël Schneider

Beilstein J. Nanotechnol. 2016, 7, 1338–1349, doi:10.3762/bjnano.7.125

• (Figure 12a) [58]. Glucose, a reducing sugar (100 mg/L), urea (100 mg/L) or Na2S (10 mg/L) only slightly decreased the photodegradation rate of Orange II at pH 7 (Figure 12b). Bovine serum albumin (BSA) (10 mg/L) and aniline (10 mg/L) had a more pronounced inhibition effect (degradation of Orange II in

Preparation of alginate–chitosan–cyclodextrin micro- and nanoparticles loaded with anti-tuberculosis compounds

• Albert Ivancic,
• Fliur Macaev,
• Fatma Aksakal,
• Veaceslav Boldescu,
• Serghei Pogrebnoi and
• Gheorghe Duca

Beilstein J. Nanotechnol. 2016, 7, 1208–1218, doi:10.3762/bjnano.7.112

• . tuberculosis H37Rv inocula were first passaged in radiometric 7H12 broth (BACTEC 12B) until the growth index (GI) reached 800–999. For the fourth replicate experiment, H37Rv was grown in 100 mL of Middlebrook 7H9 broth supplemented with 0.2% glycerol, 10% OADC (oleic acid, albumin, dextrose, catalase), and

Surface coating affects behavior of metallic nanoparticles in a biological environment

• Darija Domazet Jurašin,
• Marija Ćurlin,
• Ivona Capjak,
• Tea Crnković,
• Marija Lovrić,
• Michal Babič,
• Daniel Horák,
• Ivana Vinković Vrček and
• Srećko Gajović

Beilstein J. Nanotechnol. 2016, 7, 246–262, doi:10.3762/bjnano.7.23

• albumin (BSAAgNPs), Brij 35 (BrijAgNP) and Tween 20 (TweenAgNP). The SPIONs were prepared as uncoated γ-Fe2O3 NPs (UNSPIONs), and coated with D-mannose (MANSPIONs) or poly(L-lysine) (PLLSPIONs). Three media for NP dispersion were investigated: ultrapure water (UW), biological cell culture medium without

• broad range of mammalian cells, was used as a model biological fluid. Bovine serum albumin (BSA) served as a model serum protein due to its biological relevance and high significance in biomedical applications. Albumin is the most abundant protein in mammalian blood plasma and has outstanding buffering

• evaluation of metallic NPs in biological environments. Effect of albumin on the dispersibility of AgNPs and SPIONs in biological media When suspended in biological fluids, NPs rapidly interact with proteins that form a dynamical layer all over the NP surface, known as a protein corona (PC) [36][37][39

Au nanoparticle-based sensor for apomorphine detection in plasma

• Chiara Zanchi,
• Andrea Lucotti,
• Matteo Tommasini,
• Sebastiano Trusso,
• Ugo de Grazia,
• Emilio Ciusani and
• Paolo M. Ossi

Beilstein J. Nanotechnol. 2015, 6, 2224–2232, doi:10.3762/bjnano.6.228

• APO in blood plasma, as shown in Figure 7B. The kinetics of APO adsorption onto the gold nanostructured surface are expected to be strongly affected by matrix effects. In particular, the presence of proteins, such as human serum albumin, an abundant plasma protein that binds a wide range of drugs

Optimized design of a nanostructured SPCE-based multipurpose biosensing platform formed by ferrocene-tethered electrochemically-deposited cauliflower-shaped gold nanoparticles

• Wicem Argoubi,
• Maroua Saadaoui,
• Sami Ben Aoun and
• Noureddine Raouafi

Beilstein J. Nanotechnol. 2015, 6, 1840–1852, doi:10.3762/bjnano.6.187

• , produced in goat), bovine serum albumin (98%), ascorbic acid, dopamine, H2O2, silica gel 60 mesh and F254 nm fluorescent silica-coated aluminum TLC plates were purchased from Sigma-Aldrich (Germany) and used as received without further purification. All solvents used were of analytical grade and were used

Probing fibronectin–antibody interactions using AFM force spectroscopy and lateral force microscopy

• Andrzej J. Kulik,
• Małgorzata Lekka,
• Kyumin Lee,
• Grazyna Pyka-Fościak and
• Wieslaw Nowak

Beilstein J. Nanotechnol. 2015, 6, 1164–1175, doi:10.3762/bjnano.6.118

• for a similar type of interaction between an antigen and an antibody (i.e., bovine serum albumin and its monoclonal antibody) [35]. Our experiments do not allow for determination of which region (module) of FN interacts with Mab. As the bond dissociation is a nonequilibrium, dynamic process

Protein corona – from molecular adsorption to physiological complexity

• Lennart Treuel,
• Dominic Docter,
• Michael Maskos and
• Roland H. Stauber

Beilstein J. Nanotechnol. 2015, 6, 857–873, doi:10.3762/bjnano.6.88

• revealed a decrease of the collision efficiency (i.e., the overall number of collisions divided by the number of collisions that form an agglomerate) with an increasing protein (human serum albumin, HSA) concentration (Figure 1a). Intriguingly, they found that their colloid was stable at a point where

• further attention. Treuel and coworkers employed circular dichroism (CD) spectroscopy to study the thermodynamic and structural aspects of NP–protein interactions [47]. They investigated the formation of a serum albumin, an established model protein [7][8][9][80][111], corona around Au (13 ± 2 nm) and Ag

• the polymer shell), by live HeLa cells in the presence or absence of human transferrin (TF) and human serum albumin (HSA) in phosphate-buffered saline (PBS) medium. They studied the uptake of the NPs by quantitative confocal fluorescence microscopy. For comparison, they also studied the cellular

Influence of gold, silver and gold–silver alloy nanoparticles on germ cell function and embryo development

• Ulrike Taylor,
• Daniela Tiedemann,
• Christoph Rehbock,
• Wilfried A. Kues,
• Stephan Barcikowski and
• Detlef Rath

Beilstein J. Nanotechnol. 2015, 6, 651–664, doi:10.3762/bjnano.6.66

• ) and oligonucleotide conjugated AuNP (diameter 7.3 nm, 94 biomolecules per particle, Zeta potential −32 mV) which were tested by using bovine sperm, as well as bovine serum albumin (BSA) coated gold (diameter 6–20 nm), silver (diameter 11 nm; AgNP) and various gold silver alloy nanoparticles (silver

• concentration was 10 µg/mL and all particles were conjugated with bovine serum albumin. Reproduced with permission from [50]. Copyright 2014 Royal Society of Chemistry. Representative laser scanning microscope images of porcine cumulus–oocyte complexes after 46 h co-incubation during in vitro maturation. (A

• ) conjugated to bovine serum albumin (BSA) as measured by disc centrifugation. xc has been calculated by log-normal fitting. (B) Oocyte maturation rates after exposure to AgNP in situ or ex situ bioconjugated to BSA. *p < 0.05. Blastocyst development rates after microinjection of nanoparticles into 2-cell

Silica micro/nanospheres for theranostics: from bimodal MRI and fluorescent imaging probes to cancer therapy

• Shanka Walia and
• Amitabha Acharya

Beilstein J. Nanotechnol. 2015, 6, 546–558, doi:10.3762/bjnano.6.57

• . The silica-coated magnetic and fluorescent NPs were then conjugated with bovine serum albumin (BSA) by using N-hydroxysuccinimide (NHS) as cross linker. The synthesized NPs were then characterized by XRD, IR, TEM, absorption and fluorescence spectroscopy. The XRD diffraction peaks indicate the cubic

Increasing throughput of AFM-based single cell adhesion measurements through multisubstrate surfaces

• Miao Yu,
• Nico Strohmeyer,
• Jinghe Wang,
• Daniel J. Müller and
• Jonne Helenius

Beilstein J. Nanotechnol. 2015, 6, 157–166, doi:10.3762/bjnano.6.15

• performed with an inverted scanning confocal microscope (Axio Observer.Z1, LSM 700, Zeiss) equipped with a plan, apochromat, 25×, 0.8 numerical aperture, water-immersion objective lens (Zeiss). FITC–albumin (Sigma), fibronectin–HiLyte488 (LuBioScience), laminin–rhodamine (LuBioScience) and FITC-collagen I

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