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Search for "streptavidin" in Full Text gives 27 result(s) in Beilstein Journal of Nanotechnology.
Study of the reusability and stability of nylon nanofibres as an antibody immobilisation surface
Beilstein J. Nanotechnol. 2024, 15, 83–94, doi:10.3762/bjnano.15.8
- excess reagents. Peroxidase-labelled streptavidin was added to detect immunocaptured ricin through biotin and streptavidin binding. A fluorescent peroxidase substrate (ADH, Ampliflu) was added, and the fluorescence was measured (λemission = 530 nm and λexcitation = 590 nm). This value was divided by the
Antibody-conjugated nanoparticles for target-specific drug delivery of chemotherapeutics
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
- techniques. (a) Carbodimide coupling, (b) maleimide coupling, and (c) click coupling of antibodies on nanoparticle surfaces. Non-covalent antibody functionalization on NP surfaces using adaptor molecules (such as avidin or streptavidin). Antibody decoration strategies on nanoparticle surfaces and therapeutic
Gap-directed chemical lift-off lithographic nanoarchitectonics for arbitrary sub-micrometer patterning
Beilstein J. Nanotechnol. 2023, 14, 34–44, doi:10.3762/bjnano.14.4
- glycol undecanethiol (TEG), and biotinylated alkane PEG thiol (BAT) were purchased from Sensopath Technologies Inc. (Bozeman, MT, USA). Streptavidin was purchased from Novus Biologicals (Centennial, CO, USA). FITC-labelled antistreptavidin antibody was purchased from Jackson ImmunoResearch Inc. (West
- molecules into the post-chemical lift-off regions. After 1 h of incubation, the substrate was washed with ethanol, treated with BSA (10 mg/mL in PBS buffer) for 5 min, transferred into a streptavidin solution (50 μg/mL in PBS buffer) for 20 min, followed by FITC-labeled anti-streptavidin antibody solution
- force microscopy (Dimension Fastscan, Bruker Nano Surfaces, Hsinchu, Taiwan). Results and Discussion The results of selective SAM removal are visualized by backfilling biotinylated alkanethiol (BAT) molecules into the post lift-off regions followed by conjugating streptavidin and FITC-labeled anti
Zinc oxide nanostructures for fluorescence and Raman signal enhancement: a review
Beilstein J. Nanotechnol. 2022, 13, 472–490, doi:10.3762/bjnano.13.40
- were successfully used for the detection of relevant biological and biomedical proteins, such as bovine serum albumin and streptavidin, as well as to study the protein–protein interactions by enhanced fluorescence detection [117]. The ZnO nanoplatforms showed several key advantages, such as enhanced
Luminescent gold nanoclusters for bioimaging applications
Beilstein J. Nanotechnol. 2020, 11, 533–546, doi:10.3762/bjnano.11.42
- a fluorescent gold nanocluster immunoassay (AuNCIA) for early and sensitive detection of human immune deficiency virus (HIV) infection in vitro and HIV-infected patient samples [85]. For this study, glutathione-capped AuNCs were coupled with streptavidin (Au-SA) using EDS/NHS coupling. The strong
- noncovalent interaction between streptavidin and biotin was exploited. To achieve the immunoassay, an antibody–antigen–antibody sandwich approach was utilized (Figure 3). The substrates were first coated with capture antibodies that will interact strongly with HIV-1 p24 antigen, a target viral protein
- expressed in abundance in the early stages of HIV infection. Then, a biotinylated detection antibody was added, which resulted in a sandwich complex leaving the biotin accessible for streptavidin binding. Finally, the interaction between the biotin in the detector antibody and the streptavidin in Au-SA NCs
Evaluation of click chemistry microarrays for immunosensing of alpha-fetoprotein (AFP)
Beilstein J. Nanotechnol. 2019, 10, 2505–2515, doi:10.3762/bjnano.10.241
- -fetoprotein (AFP) is the most commonly used biomarker for early screening and diagnosis of hepatocellular carcinoma (HCC). Here, a combination of three techniques (click chemistry, the biotin–streptavidin–biotin sandwich strategy and the use of antigen–antibody interactions) were combined to implement a
- –maleimide or biotin–DBCO for the second class and biotin–amine or biotin–thiol for the third class). The anti-AFP antibody was immobilized on the surfaces via a biotin–streptavidin–biotin sandwich technique. To evaluate the sensing performance of the differently prepared surfaces, fluorescently labeled AFP
- serum of patients suffering from HCC [23]. In this study, we compare different approaches of binding chemistry for the construction of sensitive fluorescent immunosensors for AFP detection by combining the unique characteristics of click chemistry with the high sensitivity of the biotin–streptavidin
Direct growth of few-layer graphene on AlN-based resonators for high-sensitivity gravimetric biosensors
Beilstein J. Nanotechnol. 2019, 10, 975–984, doi:10.3762/bjnano.10.98
- treatment that introduces a controlled density of defects in graphene, including carboxylic groups. After that, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride/N-hydroxysuccinimide (EDC/NHS) chemistry is used to covalently bind streptavidin molecules to the surface of the sensors. The second
- functionalization protocol is based on the non-covalent bonding of streptavidin on hydrophobic graphene surfaces. The two protocols end with the effective bonding of biotinylated anti-IgG antibodies to the streptavidin, which leaves the surface of the devices ready for possible IgG detection. Keywords: biomolecule
- promotes (like carbon nanotubes [13]) the direct non-covalent binding of molecules like streptavidin, which is the basis of the functionalization scheme based on biotinylated receptors. Both methods result in short chains from the surface to the receptor, which optimizes the interaction of the acoustic
The structural and chemical basis of temporary adhesion in the sea star Asterina gibbosa
Beilstein J. Nanotechnol. 2018, 9, 2071–2086, doi:10.3762/bjnano.9.196
- the 24 lectins, 7 did not lead to a specific labelling on tube foot sections (Table 1). These lectins resulted in a very faint overall staining, as observed for the negative control (Supporting Information File 1, Figure 3F) (skipping the lectin and using only the Streptavidin-Dylight488 conjugate
- , the sections were incubated for 1 h in Dylight488-conjugated-streptavidin (Vector Laboratories) diluted 1:300 in BSA-T at room temperature. After three washing steps in TBS-T, the sections were mounted in Mowiol and analysed with a Leica DM5000 or a Zeiss Axioscope A1 microscope, or with a Leica SP5
Wafer-scale bioactive substrate patterning by chemical lift-off lithography
Beilstein J. Nanotechnol. 2018, 9, 311–320, doi:10.3762/bjnano.9.31
- -terminated hexa(ethylene glycol)undecanethiol was purchased from Nanoscience Instruments Inc. (Phoenix, AZ, USA). Streptavidin was purchased from Invitrogen Inc. (Carlsbad, CA, USA). FITC-labelled antistreptavidin antibody was purchased from Abcam Inc. (Cambridge, MA, USA). Tris(hydroxymethyl)aminomethane
- were first exposed to 10 mg/mL BSA for 5 min to reduce nonspecific protein adsorption. The patterned surfaces were then treated with 50 μg/mL streptavidin solution for 20 min followed by 20 min of 10 μg/mL FITC-labelled antistreptavidin antibody incubation. These substrates were all rinsed with
- anchoring with the FAM-labelled hairpin-structured DNA probe before (left) and after (right) target DNA introduction. (C) Sandwich-like signal reporting with the inserted probe: the CLL-treated substrate anchoring with the biotinylated thiol before (left) and after (right) the conjugation with streptavidin
Micro- and nano-surface structures based on vapor-deposited polymers
Beilstein J. Nanotechnol. 2017, 8, 1366–1374, doi:10.3762/bjnano.8.138
- same work, spatial control of the cell attachments and patterns were further produced via the biotin/streptavidin conjugation and subsequently immobilized by the cell-binding antibody [25]. A more delicate pattern formation was generated by combining the μCP technique and the supramolecular
Evaluation of quantum dot conjugated antibodies for immunofluorescent labelling of cellular targets
Beilstein J. Nanotechnol. 2017, 8, 1238–1249, doi:10.3762/bjnano.8.125
- conjugate (Qdot 625-Tubulin), and Qdot 625 conjugated to streptavidin (Qdot-Streptavidin). We found that while the prototypical target of Qdot-Abs: tubulin, could be easily labelled, several other protein targets including nuclear proteins and components of large cytosolic protein complexes could not be
- antibody (Figure S15 in Supporting Information File 1), with the similar results obtained as for Qdot 625-Ab. An alternative Qdot 625 conjugated to the biotin-binding protein streptavidin (Qdot-Streptavidin) (Thermo Fisher Scientific, UK) was also evaluated. To test the specificity of Qdot-Streptavidin for
- antibody, and Qdot-Streptavidin. All of the endogenous biotin sites in the cell were blocked before addition of the biotinylated anti-GFP primary antibody with an endogenous biotin-blocking kit (Thermo Fisher Scientific, UK). Similar results were obtained as previously for Qdot 625-Ab, with Qdot
Phospholipid arrays on porous polymer coatings generated by micro-contact spotting
Beilstein J. Nanotechnol. 2017, 8, 715–722, doi:10.3762/bjnano.8.75
- steps, while still being accessible for protein and antibody binding. To characterize binding to polymer-embedded lipids we have applied Streptavidin as well as biologically important biotinylated androgen receptor binding onto 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine-N-(cap biotinyl) (Biotinyl
- arrays we selected lipid–protein pairs applied in previous settings: Biotin-Cap-PE and streptavidin labeled with Cy3 dye (STV-Cy3) as a simple protein model; and DNP-cap-PE with anti-DNP IgE as a model for allergen/antibody recognition. These interactions are well-characterized for biomimetic lipid
- fluorescence as the ink below the feature surface also contributes to the signal. Protein and antibody binding onto lipid arrays The selective binding of proteins to the lipid arrays on HEMA polymer was first tested using fluorophore labelled streptavidin (STV-FITC) for the coupling with biotin headgroups
Comparison of four functionalization methods of gold nanoparticles for enhancing the enzyme-linked immunosorbent assay (ELISA)
Beilstein J. Nanotechnol. 2017, 8, 244–253, doi:10.3762/bjnano.8.27
- impact in several fields. In this respect, many methods have been developed for improving the technique, ranging from fluorescence substrates to methods for increasing the number of enzyme molecules involved in the detection such as the biotin–streptavidin method. In this context, nanotechnology has
Streptavidin-coated gold nanoparticles: critical role of oligonucleotides on stability and fractal aggregation
Beilstein J. Nanotechnol. 2017, 8, 1–11, doi:10.3762/bjnano.8.1
- Andrea Doria 6, I-95125, Catania, Italy 10.3762/bjnano.8.1 Abstract Gold nanoparticles (AuNPs) exhibit unique properties that can be modulated through a tailored surface functionalization, enabling their targeted use in biochemical sensing and medical diagnostics. In particular, streptavidin-modified
- AuNPs are increasingly used for biosensing purposes. We report here a study of AuNPs surface-functionalized with streptavidin-biotinylated oligonucleotide, focussing on the role played by the oligonucleotide probes in the stabilization/destabilization of the functionalized nanoparticle dispersion. The
- thorough understanding of the fundamental properties of bioconjugated AuNPs is of great importance for the design of highly sensitive and reliable functionalized AuNP-based assays. Keywords: biosensors; DNA; gold nanoparticles; nanoparticles aggregation; plasmonics; streptavidin; Introduction Gold
A novel electrochemical nanobiosensor for the ultrasensitive and specific detection of femtomolar-level gastric cancer biomarker miRNA-106a
Beilstein J. Nanotechnol. 2016, 7, 2023–2036, doi:10.3762/bjnano.7.193
- shown in Figure 1. After synthesis of gold–magnetic NPs as a three-layer nanocomposite, these particles were covalently coated with streptavidin by using 11-mercaptoundecanoic acid (MUA) and carbodiimide hydrochloride/N-hydroxysulfosuccinimide (EDC/NHS). Next, P1 was immobilized on NPs through
- streptavidin–biotin interaction. In parallel, the working area of SPCE was covered by streptavidin and then exposed to P2. In order to quantify miR-106a in samples, the target was first captured by gold–magnetic nanoprobes and then hybridized with P2 immobilized on the electrode. The final detection was
- strategies such as using the thiol group, particle functionalization, and streptavidin–biotin interaction. Streptavidin has an extraordinary high affinity for biotin and the streptavidin–biotin bond is one of the strongest non-covalent interactions known in nature (with a dissociation constant in the order
Novel roles for well-known players: from tobacco mosaic virus pests to enzymatically active assemblies
Beilstein J. Nanotechnol. 2016, 7, 613–629, doi:10.3762/bjnano.7.54
- combined the covalent coupling of biotinylated linkers to a tailored virus variant, and subsequent bioaffinity binding of commercially available streptavidin [SA]-enzyme conjugates (Figure 5A). A genetically modified TMV (TMVCys) with a cysteine residue (S3C) surface-exposed nearby every CP N-terminus [61
Functional fusion of living systems with synthetic electrode interfaces
Beilstein J. Nanotechnol. 2016, 7, 296–301, doi:10.3762/bjnano.7.27
- detector enhancing material contrast (Figure 1b, 3) and accessibility of the gold surface demonstrated by specific labelling with a biotin and AlexaFluor 488 labelled streptavidin, resulting in punctured fluorescence signals at the expected density (Figure 1b, 3, inset). By use of a profilometer (see
- ). The accessibility of the gold surface is proven by fluorescence microscopy analysis of NEIs in which gold was labeled by a biotin- and AlexaFluor488-labeled streptavidin (b, 3, inset). A SEM side view obtained at a centric braking edge reveals the composition of the interface illustrating gold pillars
Single-molecule mechanics of protein-labelled DNA handles
Beilstein J. Nanotechnol. 2016, 7, 138–148, doi:10.3762/bjnano.7.16
- ) were conjugated with streptavidin or neutravidin proteins. The DIG-modified ends of these hybrids were bound to surface-modified polystyrene (anti-DIG) beads. Using different physiological buffers, optical force measurements showed consistent mechanical characteristics with long dissociation times
- . These protein-modified DNA hybrids were also interconnected in situ with other tethered biotinylated DNA molecules. Electron-multiplying CCD (EMCCD) imaging control experiments revealed that quantum dot–streptavidin conjugates at the end of DNA handles remain freely accessible. The experiments presented
- present a novel assay for reliably producing protein-labelled DNA hybrids (PDHs) to be used as molecular spacers and handles, exhibiting the necessary stability for time-critical displacement and force measurements. Streptavidin and neutravidin were used for protein labelling, acting as a molecular
Orthogonal chemical functionalization of patterned gold on silica surfaces
Beilstein J. Nanotechnol. 2015, 6, 2272–2277, doi:10.3762/bjnano.6.233
- biotinylated thiols and antifouling PEG/silanes. A similar approach was already used to direct the immobilization of streptavidin-coated nanoparticles [31] onto the gold nanostructures. Here, “single” (i.e., not adsorbed on beads) proteins were immobilized as shown in Figure 5. Conclusion The orthogonal
- protein incubation and shows a height consistent with the deposition of 8 nm Ti + 30 nm Au. The streptavidin sample (black) was orthogonally functionalized and subjected to protein immobilization. The increase in size is indicative of the binding of streptavidin on the nanostructure. Thiol/silane mixtures
Probing fibronectin–antibody interactions using AFM force spectroscopy and lateral force microscopy
Beilstein J. Nanotechnol. 2015, 6, 1164–1175, doi:10.3762/bjnano.6.118
- –streptavidin [8], or lectin–carbohydrate [9]. Direct measurements of intermolecular forces for complementary DNA strands have been carried out as well [10]. Protein–antibody interactions are of particular interest in immunochemical-based diagnosis [11]. Therefore, studies of the interaction forces provide
Silica micro/nanospheres for theranostics: from bimodal MRI and fluorescent imaging probes to cancer therapy
Beilstein J. Nanotechnol. 2015, 6, 546–558, doi:10.3762/bjnano.6.57
- chloride salts of rare earth and lanthanide metals, namely yttrium (Y), ytterbium (Yb) and erbium (Er) in presence of EDTA solution. The silica coating of these NPs was done by hydrolysis of TEOS and APS followed by conjugation of streptavidin on the silica surface. The TEM micrographs revealed that the
- /g, respectively, whereas that of ferrofluid magnetic NPs was found to be 65 emu/g. The immobilization of streptavidin on the silica surface was confirmed by protein assay study on biotinylated goat anti-human IgG. Also, Choi et al. [34] reported the synthesis of magnetic and fluorescent inorganic
Hematopoietic and mesenchymal stem cells: polymeric nanoparticle uptake and lineage differentiation
Beilstein J. Nanotechnol. 2015, 6, 383–395, doi:10.3762/bjnano.6.38
- ) supplemented with 10% fetal calf serum (FCS, Invitrogen), 100 units penicillin and 100 µg/mL medium streptavidin (Invitrogen) were used. For cultivation and differentiation, the cells were kept in a humidified incubator with 5% CO2 at 37 °C. All experiments were performed with cells incubated with 300 µg/mL
- hMSCs were generated as previously described [36]. MSC were cultivated in α–MEM (Lonza, Cologne, Germany) supplemented with 20% fetal calf serum (FCS, Invitrogen, Karlsruhe, Germany), 100 units penicillin and 100 µg/mL medium streptavidin (Invitrogen), 1 mM pyruvate (Invitrogen) and 0.6% ciprofloxacin
The effect of surface charge on nonspecific uptake and cytotoxicity of CdSe/ZnS core/shell quantum dots
Beilstein J. Nanotechnol. 2015, 6, 281–292, doi:10.3762/bjnano.6.26
- biotinylated QDs [30], or to observe the movement of single, streptavidin-coated QDs along microtubules [31]. Results and Discussion ECIS and the MTS assay were used to evaluate the viability of MDCKII cells exposed to CdSe/ZnS QDs functionalized with positively-charged CA ligands, negatively-charged DHLA- or
Functionalization of α-synuclein fibrils
Beilstein J. Nanotechnol. 2015, 6, 124–133, doi:10.3762/bjnano.6.12
- attach to one fibril, when two neutravidin molecules that are present on the surface of gold nanoparticle bind to biotin moieties on the same fibril. The application of the biotin–streptavidin (avidin) interaction, which is known to be one of the strongest interactions in nature, offers a broad range of
- possibilities with respect to functionalization of fibrils, since many streptavidin-conjugated components (enzymes and metal nanoparticles) are already available. Depending on the final aim, two strategies for functionalization may be used since the modifications can be performed before or after fibrillation
Coating with luminal gut-constituents alters adherence of nanoparticles to intestinal epithelial cells
Beilstein J. Nanotechnol. 2014, 5, 2308–2315, doi:10.3762/bjnano.5.239
- . The biotinylated lectin RCA I was used in a concentration of 20 µg/mL in 0.2% gelatin/PBS to label the cells over night at 4 °C. Afterwards the cells were incubated with Cy5-conjugated streptavidin (GE Healthcare, Brand Amersham, Pittsburgh, USA), 5 µg/mL in 0.2% gelatin/PBS, for 90 min at rt. Finally
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