Classification and application of metal-based nanoantioxidants in medicine and healthcare

• Nguyen Nhat Nam,
• Nguyen Khoi Song Tran,
• Tan Tai Nguyen,
• Nguyen Ngoc Trai,
• Nguyen Phuong Thuy,
• Hoang Dang Khoa Do,
• Nhu Hoa Thi Tran and
• Kieu The Loan Trinh

Beilstein J. Nanotechnol. 2024, 15, 396–415, doi:10.3762/bjnano.15.36

• than copper content and size. The enzyme activity of natural CAT highly depends on the three-dimensional (3D) structure of the protein. A significant decrease or even loss of CAT activity can be caused already by small changes in the protein conformation and structure. As a matter of fact, cellular

Multiscale modelling of biomolecular corona formation on metallic surfaces

• Parinaz Mosaddeghi Amini,
• Ian Rouse,
• Julia Subbotina and
• Vladimir Lobaskin

Beilstein J. Nanotechnol. 2024, 15, 215–229, doi:10.3762/bjnano.15.21

• orientation of each individual protein, a primary coarse-graining step was performed. In this part, we use the UA model to predict the protein–NP binding energies. This model takes into account various factors, such as the material’s chemical composition, size, shape, surface roughness, charge

Study of the reusability and stability of nylon nanofibres as an antibody immobilisation surface

• Inés Peraile,
• Matilde Gil-García,
• Laura González-López,
• Nushin A. Dabbagh-Escalante,
• Juan C. Cabria-Ramos and
• Paloma Lorenzo-Lozano

Beilstein J. Nanotechnol. 2024, 15, 83–94, doi:10.3762/bjnano.15.8

• nanofibres with well-oriented antibodies anchored by protein A/G. Our study shows that stripping with glycine buffer pH 2.5 allows the nanofibres to be reused as long as protein A/G has been previously anchored, leaving both nanofibre and protein A/G unchanged. On the other hand, we investigated the

• and Discussion Results of nanofibre reusability study High-salinity antigen/antibody (Ag/Ac) elution buffer pH 6.6 as stripping agent A commercial Ag/Ac elution buffer pH 6.6 with high salinity was able to remove almost all antibody fixed on the nanofibres through protein A/G (88.6%). The retained

• antibody captured by the NFs via protein A/G (93.4%) since the retained antibody after stripping treatment (group 2) was only 6.6% compared to group 1 (Figure 3). However, the ammonium hydroxide buffer pH 11 interfered with the reconstituted immunocapture system to such an extent that only 31.5% of the

Antibody-conjugated nanoparticles for target-specific drug delivery of chemotherapeutics

• Mamta Kumari,
• Amitabha Acharya and
• Praveen Thaggikuppe Krishnamurthy

Beilstein J. Nanotechnol. 2023, 14, 912–926, doi:10.3762/bjnano.14.75

• binding, nonglycosylated and neutral forms of avidin, either natural or recombinant, are used (e.g., streptavidin and neutravidin) [45][64]. Another method to achieve oriented immobilization of antibodies is based upon the use of Fc binding proteins (such as protein-G and protein-A), which have ability to

DNA aptamer selection and construction of an aptasensor based on graphene FETs for Zika virus NS1 protein detection

• Nathalie B. F. Almeida,
• Thiago A. S. L. Sousa,
• Viviane C. F. Santos,
• Camila M. S. Lacerda,
• Thais G. Silva,
• Rafaella F. Q. Grenfell,
• Flavio Plentz and
• Antero S. R. Andrade

Beilstein J. Nanotechnol. 2022, 13, 873–881, doi:10.3762/bjnano.13.78

• of ZIKV NS1 protein. (a) Representative curves of the normalized graphene resistance (RSD) as a function of the gate voltage (VG) before (black line) and after (red line) functionalization with ZIKV60 aptamers. These measurements were carried out using 100 mM PBS as electrolyte for gating. (b

Photothermally active nanoparticles as a promising tool for eliminating bacteria and biofilms

• Mykola Borzenkov,
• Piersandro Pallavicini,
• Angelo Taglietti,
• Laura D’Alfonso,
• Maddalena Collini and
• Giuseppe Chirico

Beilstein J. Nanotechnol. 2020, 11, 1134–1146, doi:10.3762/bjnano.11.98

• engineered to combat bacterial infections by integrating bacterial conjugation and NIR-triggered photothermal sterilization [97]. In a very recent publication, polyethylene glycol (PEG)-MoS2 nanosheets additionally functionalized with an antibody (anti-protein A lgG) and polydopamine were applied to induce

Multilayer capsules made of weak polyelectrolytes: a review on the preparation, functionalization and applications in drug delivery

• Varsha Sharma and
• Anandhakumar Sundaramurthy

Beilstein J. Nanotechnol. 2020, 11, 508–532, doi:10.3762/bjnano.11.41

• section, the antibodies were used to functionalize PVPAlk low fouling capsules using covalent click chemistry to target cancer cells [101]. They were very effective against LIM2405 colorectal cancer cells even at a low concentration of 0.1% cancer cells in the total cell population. Protein A (obtained

• from Staphylococcus aureus) was adsorbed on PGA/PLL film via electrostatic attraction and the in vitro cell contact with this protein mainly occurred via local film degradation [103]. The antitumoral, antitoxic, anticarcenogenic, antifungal and antiparasitic properties of protein A could be a good

Targeting strategies for improving the efficacy of nanomedicine in oncology

• Gonzalo Villaverde and
• Alejandro Baeza

Beilstein J. Nanotechnol. 2019, 10, 168–181, doi:10.3762/bjnano.10.16

• antibody attachment with a high precision level [29]. Another interesting strategy is the attachment of protein A on the nanoparticle surface prior to the incorporation of the antibody [30]. Protein A is a membrane protein produced by Staphylococcus aureus in order to complex the immunoglobulins by the

• complement region (Fc) deactivating the immune attack of the host. Thus, antibodies can be anchored to the surface of a nanoparticle decorated with protein A thanks to the strong affinity between the protein and the Fc region, which is not involved in the recognition process and therefore, this process

Novel roles for well-known players: from tobacco mosaic virus pests to enzymatically active assemblies

• Claudia Koch,
• Fabian J. Eber,
• Carlos Azucena,
• Alexander Förste,
• Stefan Walheim,
• Thomas Schimmel,
• Alexander M. Bittner,
• Holger Jeske,
• Hartmut Gliemann,
• Sabine Eiben,
• Fania C. Geiger and
• Christina Wege

Beilstein J. Nanotechnol. 2016, 7, 613–629, doi:10.3762/bjnano.7.54

• antibodies as “molecular stickers” and thus spacers was developed into a partially universal coupling concept to viral templates [88]: It allows for the stable binding of functional proteins fused with the Z33 peptide (derived from staphylococcal protein A [164]) to the Fc portions of immunoglobulins IgG1

• equipped with commercially available, fully active enzyme preparations at so far unsurpassed surface densities; their performance was even stabilized over weeks. Antibodies were installed with high efficiencies on TMV backbones as well, by protein A-exposing CP variants or suitable affinity tags. In

Functionalization of α-synuclein fibrils

• Simona Povilonienė,
• Vida Časaitė,
• Virginijus Bukauskas,
• Arūnas Šetkus,
• Juozas Staniulis and
• Rolandas Meškys

Beilstein J. Nanotechnol. 2015, 6, 124–133, doi:10.3762/bjnano.6.12

• ANX column and reloaded into a Q XL column. A typical yield from 1 L of culture was 30 mg of the homogenous protein. A band corresponding to an 18 kDa protein was observed in 15% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) (Figure 1). The theoretical molecular mass of α

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

• proteins, HSAam and HSAsuc, have a larger fraction of positive and negative regions, respectively, than the native protein. A small, negatively charged metal NP is likely to find a small region with a positive surface charge, whereas the larger footprint of a QD will average over negative and positive

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

Atomic force microscopy recognition of protein A on Staphylococcus aureus cell surfaces by labelling with IgG–Au conjugates

• Elena B. Tatlybaeva,
• Hike N. Nikiyan,
• Alexey S. Vasilchenko and
• Dmitri G. Deryabin

Beilstein J. Nanotechnol. 2013, 4, 743–749, doi:10.3762/bjnano.4.84

• /bjnano.4.84 Abstract The labelling of functional molecules on the surface of bacterial cells is one way to recognize the bacteria. In this work, we have developed a method for the selective labelling of protein A on the cell surfaces of Staphylococcus aureus by using nanosized immunogold conjugates as

• cell-surface markers for atomic force microscopy (AFM). The use of 30-nm size Au nanoparticles conjugated with immunoglobulin G (IgG) allowed the visualization, localization and distribution of protein A–IgG complexes on the surface of S. aureus. The selectivity of the labelling method was confirmed in

• mixtures of S. aureus with Bacillus licheniformis cells, which differed by size and shape and had no IgG receptors on the surface. A preferential binding of the IgG–Au conjugates to S. aureus was obtained. Thus, this novel approach allows the identification of protein A and other IgG receptor-bearing

Mapping mechanical properties of organic thin films by force-modulation microscopy in aqueous media

• Jianming Zhang,
• Zehra Parlak,
• Carleen M. Bowers,
• Terrence Oas and
• Stefan Zauscher

Beilstein J. Nanotechnol. 2012, 3, 464–474, doi:10.3762/bjnano.3.53

• domain of staphylococcal protein A. Protein A is a surface protein found on the cell wall of staphylococcus aureus bacteria and contains five domains for IgG-binding (SpA-N). One of the domains is named the B-domain and its structure and folding behavior have been well studied [54]. Specifically, we use

• thermal evaporator (Kurt Lesker PVD 75), and subsequently cleaned by ozone plasma ashing (Emitech K-1050X). Protein monolayer Five tandem B-domains of staphylococcal protein A were expressed and purified from E. coli. The C-terminus of the terminal protein was modified with cysteine to enable protein