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Relevant bibliographies by topics / Biotin-Streptavidin

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Academic literature on the topic 'Biotin-Streptavidin'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

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Journal articles on the topic "Biotin-Streptavidin"

1

Wu, Sau-Ching, and Sui-Lam Wong. "Engineering of a Bacillus subtilis Strain with Adjustable Levels of Intracellular Biotin for Secretory Production of Functional Streptavidin." Applied and Environmental Microbiology 68, no. 3 (March 2002): 1102–8. http://dx.doi.org/10.1128/aem.68.3.1102-1108.2002.

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ABSTRACT Streptavidin is a biotin-binding protein which has been widely used in many in vitro and in vivo applications. Because of the ease of protein recovery and availability of protease-deficient strains, the Bacillus subtilis expression-secretion system is an attractive system for streptavidin production. However, attempts to produce streptavidin using B. subtilis face the problem that cells overproducing large amounts of streptavidin suffer poor growth, presumably because of biotin deficiency. This problem cannot be solved by supplementing biotin to the culture medium, as this will saturate the biotin binding sites in streptavidin. We addressed this dilemma by engineering a B. subtilis strain (WB800BIO) which overproduces intracellular biotin. The strategy involves replacing the natural regulatory region of the B. subtilis chromosomal biotin biosynthetic operon (bioWAFDBIorf2) with an engineered one consisting of the B. subtilis groE promoter and gluconate operator. Biotin production in WB800BIO is induced by gluconate, and the level of biotin produced can be adjusted by varying the gluconate dosage. A level of gluconate was selected to allow enhanced intracellular production of biotin without getting it released into the culture medium. WB800BIO, when used as a host for streptavidin production, grows healthily in a biotin-limited medium and produces large amounts (35 to 50 mg/liter) of streptavidin, with over 80% of its biotin binding sites available for future applications.

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Stayton, Patrick S., Stefanie Freitag, Lisa A. Klumb, Ashutosh Chilkoti, Vano Chu, Julie E. Penzotti, Richard To, et al. "Streptavidin–biotin binding energetics." Biomolecular Engineering 16, no. 1-4 (December 1999): 39–44. http://dx.doi.org/10.1016/s1050-3862(99)00042-x.

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3

Soltani, Orkide, Mohammad Reza Bozorgmehr, and Mohammad Momen-Heravi. "Does the single-walled carbon nanotube affect the rate constant of binding of biotin to streptavidin? Molecular dynamics simulation perspective." Progress in Reaction Kinetics and Mechanism 44, no. 3 (June 18, 2019): 234–43. http://dx.doi.org/10.1177/1468678319825710.

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The interaction of biotin and streptavidin in the presence and absence of a carbon nanotube was studied by molecular dynamics simulation. With respect to the Arrhenius dependence of the rate constants with temperature, those of streptavidin–biotin complex formation ([Formula: see text]) and streptavidin–biotin complex dissociation ([Formula: see text]) were calculated from molecular dynamics simulation trajectories. Nanotube has reduced the amount of and k1and k1. However, the biotin position in streptavidin does not change much. The results obtained from MMPBSA calculations show that the contribution of the van der Waals forces to both systems (in the absence and presence of the nanotube) was greater than that of electrostatic forces. The presence of the nanotube also led to the reduction of van der Waals and electrostatic forces in the interaction of biotin with streptavidin. However, this reduction was greater for electrostatic forces. In the absence of a nanotube, there are four hydrogen bonds between streptavidin and biotin, which are related to the residues Ser27, Tyr43, Ser45 and Ser88. In the presence of the nanotube, the hydrogen bonding of biotin with Ser45 is removed.

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4

De Odrowaz Piramowicz, Marzena, Paweł Czuba, Marta Targosz, Kvetoslava Burda, and Marek Szymoński. "Dynamic force measurements of avidin-biotin and streptavdin-biotin interactions using AFM." Acta Biochimica Polonica 53, no. 1 (January 12, 2006): 93–100. http://dx.doi.org/10.18388/abp.2006_3367.

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Using atomic force microscopy (AFM) we performed dynamic force measurements of the adhesive forces in two model systems: avidin-biotin and streptavidin-biotin. In our experiments we used glutaraldehyde for immobilization of (strept)avidin on the tip and biotin on the sample surface. Such interface layers are more rigid than those usually reported in the literature for AFM studies, when (strept)avidin is coupled with biotinylated bovine albumin and biotin with agarose polymers. We determined the dependence of the rupture forces of avidin-biotin and streptavidin-biotin bonds in the range 300-9600 pN/s. The slope of a semilogarithmic plot of this relation changes at about 1700 pN/s. The existence of two different regimes indicates the presence of two activation barriers of these complexes during the dissociation process. The dissociation rates and activation energy barriers, calculated from the Bell model, for the avidin-biotin and streptavidin-biotin interactions are similar to each other for loading rates > 1700 pN/s but they are different from each other for loading rates < 1700 pN/s. In the latter case, the dissociation rates show a higher stability of the avidin-biotin complex than the streptavidin-biotin complex due to a larger outer activation barrier of 0.8 k(B)T. The bond-rupture force is about 20 pN higher for the avidin-biotin pair than for the streptavidin-biotin pair for loading rates < 1700 pN/s. These two experimental observations are in agreement with the known structural differences between the biotin binding pocket of avidin and of streptavidin.

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5

Zhu, Xianwei, and Hiroaki Shinohara. "Fluorescence Enhancement of Fluorescent Unnatural Streptavidin by Binding of a Biotin Analogue with Spacer Tail and Its Application to Biotin Sensing." Scientific World Journal 2014 (2014): 1–6. http://dx.doi.org/10.1155/2014/165369.

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We designed a novel molecular biosensing system for the detection of biotin, an important vitamin by the combination of fluorescent unnatural streptavidin with a commercialized biotin-(AC5)2-hydrazide. A fluorescent unnatural amino acid, BODIPY-FL-aminophenylalanine (BFLAF), was position-specifically incorporated into Trp120 of streptavidin by four-base codon method. Fluorescence of the Trp120BFLAF mutant streptavidin was enhanced by the addition of biotin-(AC5)2-hydrazide with the concentration dependent, whereas fluorescence enhancement was not observed at all by the addition of natural biotin. It was considered that the spacer tail of biotin-(AC5)2-hydrazide may disturb the fluorescence quenching of the Trp120BFLAF by Trp79 and Trp108 of the neighbor subunit. Therefore, biotin sensing was carried out by the competitive binding reaction of biotin-(AC5)2-hydrazide and natural biotin to the fluorescent mutant streptavidin. The fluorescence intensity decreased by increasing free biotin concentration. The result suggested that molecular biosensor for small ligand could be successfully designed by the pair of fluorescent mutant binding protein and ligand analogue.

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6

Gitlin, G., E. A. Bayer, and M. Wilchek. "Studies on the biotin-binding site of streptavidin. Tryptophan residues involved in the active site." Biochemical Journal 256, no. 1 (November 15, 1988): 279–82. http://dx.doi.org/10.1042/bj2560279.

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Streptavidin, the non-glycosylated bacterial analogue of the egg-white glycoprotein avidin, was modified with the tryptophan-specific reagent 2-hydroxy-5-nitrobenzyl (Hnb) bromide. As with avidin, complete loss of biotin-binding activity was achieved upon modification of an average of one tryptophan residue per streptavidin subunit. Tryptic peptides obtained from an Hnb-modified streptavidin preparation were fractionated by reversed-phase h.p.l.c., and three major Hnb-containing peptide fractions were isolated. Amino acid and N-terminal sequence analysis revealed that tryptophan residues 92, 108 and 120 are modified and probably comprise part of the biotin-binding site of the streptavidin molecule. Unlike avidin, the modification of lysine residues in streptavidin failed to result in complete loss of biotin-binding activity. The data imply subtle differences in the fine structure of the respective biotin-binding sites of the two proteins.

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7

Jeon, Byeong Jun, Sulhee Kim, Min-Seok Kim, Ji-Ho Lee, Beom Seok Kim, and Kwang Yeon Hwang. "Insights into the structure of mature streptavidin C1 from Streptomyces cinnamonensis reveal the self-binding of the extension C-terminal peptide to biotin-binding sites." IUCrJ 8, no. 2 (January 11, 2021): 168–77. http://dx.doi.org/10.1107/s2052252520015675.

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The members of the avidin protein family are well known for their high affinity towards D-biotin and their structural stability. These properties make avidins a valuable tool for various biotechnological applications. In the present study, two avidin-like biotin-binding proteins (named streptavidin C1 and C2) from Streptomyces cinnamonensis were newly identified while exploring antifungal proteins against Fusarium oxysporum f. sp. cucumerinum. Streptavidin C1 reveals a low correlation (a sequence identity of approximately 64%) with all known streptavidins, whereas streptavidin C2 shares a sequence identity of approximately 94% with other streptavidins. Here, the crystal structures of streptavidin C1 in the mature form and in complex with biotin at 2.1 and 2.5 Å resolution, respectively, were assessed. The overall structures present similar tetrameric features with D 2 symmetry to other (strept)avidin structures. Interestingly, the long C-terminal region comprises a short α-helix (C-Lid; residues 169–179) and an extension C-terminal peptide (ECP; residues 180–191) which stretches into the biotin-binding sites of the same monomer. This ECP sequence (–180VTSANPPAS188–) is a newly defined biotin-binding site, which reduces the ability to bind to (strept)avidin family proteins. The novel streptavidin C1 could help in the development of an engineered tetrameric streptavidin with reduced biotin-binding capacity as well as other biomaterial tools.

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8

Buckland, R. M. "Strong signals from streptavidin–biotin." Nature 320, no. 6062 (April 1986): 557–58. http://dx.doi.org/10.1038/320557a0.

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9

González, Martín, Luis A. Bagatolli, Izaskun Echabe, Jose L. R. Arrondo, Carlos E. Argaraña, Charles R. Cantor, and Gerardo D. Fidelio. "Interaction of Biotin with Streptavidin." Journal of Biological Chemistry 272, no. 17 (April 25, 1997): 11288–94. http://dx.doi.org/10.1074/jbc.272.17.11288.

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10

Maeda, Yoshiaki, Tomoko Yoshino, Masaaki Takahashi, Harumi Ginya, Junko Asahina, Hideji Tajima, and Tadashi Matsunaga. "Noncovalent Immobilization of Streptavidin on In Vitro- and In Vivo-Biotinylated Bacterial Magnetic Particles." Applied and Environmental Microbiology 74, no. 16 (June 20, 2008): 5139–45. http://dx.doi.org/10.1128/aem.00618-08.

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ABSTRACT Biotinylated magnetic nanoparticles were constructed by displaying biotin acceptor peptide (BAP) or biotin carboxyl carrier protein (BCCP) on the surface of bacterial magnetic particles (BacMPs) synthesized by Magnetospirillum magneticum AMB-1. BAP-displaying BacMPs (BAP-BacMPs) were extracted from bacterial cells and incubated with biotin and Escherichia coli biotin ligase. Then the in vitro biotinylation of BAP-BacMPs was confirmed using alkaline phosphatase-labeled antibiotin antibody. In contrast, BacMPs displaying the intact 149 residues of AMB-1 BCCP (BCCP-BacMPs) and displaying the COOH-terminal 78 residues of BCCP (BCCP78-BacMPs) were biotinylated in AMB-1 cells. The in vivo biotinylation of BCCP-BacMPs and BCCP78-BacMPs was thought to be performed by endogenous AMB-1 biotin ligase. Streptavidin was introduced onto biotinylated BacMPs by simple mixing. In an analysis using tetramethyl rhodamine isocyanate-labeled streptavidin, approximately 15 streptavidin molecules were shown to be immobilized on a single BCCP-BacMP. Furthermore, gold nanoparticle-BacMP composites were constructed via the biotin-streptavidin interaction. The conjugation system developed in this work provides a simple, low-cost method for producing biotin- or streptavidin-labeled magnetic nanoparticles. Various functional materials can be site selectively immobilized on these specially designed BacMPs. By combining the site-selective biotinylation technology and the protein display technology, more innovative and attractive magnetic nanomaterials can be constructed.

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Dissertations / Theses on the topic "Biotin-Streptavidin"

1

Chu, Vano. "Molecular recognition in the streptavidin-biotin system /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/8106.

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Hamblett, Kevin James. "Optimization of pretargeted radioimmunotherapy /." Thesis, Connect to this title online; UW restricted, 2002. http://hdl.handle.net/1773/8077.

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3

Sedlak, Steffen Matthias [Verfasser], and Hermann [Akademischer Betreuer] Gaub. "Mechanics of the streptavidin/biotin interaction / Steffen Matthias Sedlak ; Betreuer: Hermann Gaub." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2019. http://d-nb.info/1218970901/34.

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Moore, Adam. "On biomolecular interactions : investigating receptor-ligand interactions; theoretical and experimental approaches." Thesis, University of Nottingham, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.298073.

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Domingo, Rommel J. "Pre-targeted radioimmunotherapy with streptavidin-CC49 monoclonal antibody and §9§0Y-DOTA-biotin." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ29337.pdf.

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6

Shimoboji, Tsuyoshi. "Photo-switching of protein activities by conjugation of photo-responsive polymers to proteins /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/8097.

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Schendel, Leonard C. [Verfasser], and Hermann [Akademischer Betreuer] Gaub. "Tether and reinforcement effects on Streptavidin-Biotin, and induced binding in nanoapertures / Leonard C. Schendel ; Betreuer: Hermann Gaub." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2020. http://d-nb.info/1214593380/34.

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8

Shea, Jessica Anna-Marie. "Streptavidin-biotin binding of DNA amplicons: methods for the typing and re-typing of forensically relevant short tandem repeats." Thesis, Boston University, 2012. https://hdl.handle.net/2144/12621.

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Thesis (M.S.)--Boston University
Submission of evidentiary samples to DNA units for exhaustive testing is becoming commonplace. For these samples, only one attempt at amplification is possible. However, more than one amplification may be necessary if the condition of the DNA causes poor amplification, more than one type of STR kit testing is required, or if there is an instrument malfunction during amplification. Current research into the re-amplification of already amplified samples focuses on placing the PCR product back into the thermal cycler with new reagents for additional cycles. These methods typically result in outcomes which are unsatisfactory for forensic purposes. As a result, there is a need for a forensic method capable of recovering the original template DNA for purposes of re-amplification. This study outlines the development of a novel method to recover the original template DNA in a condition that allows for re-amplification using new STR loci. A dynamic model was designed to assist in the experimental optimization. Amplification was performed using biotinylated primers and the post PCR 'work product' was subsequently cleaned using streptavidin coated magnetic beads to remove the STR amplicons. Centrifugal filtration followed in order to remove any remaining primers and salts that may interfere with re-amplification. Re-amplification was then performed with non-biotinylated primers. Re-amplification of the template DNA using a new STR locus was successful, making the amplification of limited DNA samples non-destructive and the notion of 'exhaustive DNA typing' obsolete.

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9

Luschtinetz, Franziska. "Cyaninfarbstoffe als Fluoreszenzsonden in biomimetischen und biologischen Systemen : Fluoreszenz-Korrelations-Spektroskopie und Fluoreszenzanisotropie-Untersuchungen." Phd thesis, Universität Potsdam, 2010. http://opus.kobv.de/ubp/volltexte/2010/4847/.

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Um Prozesse in biologischen Systemen auf molekularer Ebene zu untersuchen, haben sich vor allem fluoreszenzspektroskopische Methoden bewährt. Die Möglichkeit, einzelne Moleküle zu beobachten, hat zu einem deutlichen Fortschritt im Verständnis von elementaren biochemischen Prozessen geführt. Zu einer der bekanntesten Methoden der Einzelmolekülspektroskopie zählt die Fluoreszenz-Korrelations-Spektroskopie (FCS), mit deren Hilfe intramolekulare und diffusionsgesteuerte Prozesse in einem Zeitbereich von µs bis ms untersucht werden können. Durch die Verwendung von sog. Fluoreszenzsonden können Informationen über deren molekulare Mikroumgebung erhalten werden. Insbesondere für die konfokale Mikroskopie und die Einzelmolekülspektroskopie werden Fluoreszenzfarbstoffe mit einer hohen Photostabilität und hohen Fluoreszenzquantenausbeute benötigt. Aufgrund ihrer hohen Fluoreszenzquantenausbeute und der Möglichkeit, maßgeschneiderte“ Farbstoffe in einem breiten Spektralbereich für die Absorption und Fluoreszenz zu entwickeln, sind Cyaninfarbstoffe von besonderem Interesse für bioanalytische Anwendungen. Als Fluoreszenzmarker finden diese Farbstoffe insbesondere in der klinischen Diagnostik und den Lebenswissenschaften Verwendung. Die in dieser Arbeit verwendeten Farbstoffe DY-635 und DY-647 sind zwei typische Vertreter dieser Farbstoffklasse. Durch Modifizierung können die Farbstoffe kovalent an biologisch relevante Moleküle gebunden werden. Aufgrund ihres Absorptionsmaximums oberhalb von 630nm werden sie insbesondere in der Bioanalytik eingesetzt. In der vorliegenden Arbeit wurden die spektroskopischen Eigenschaften der Cyaninfarbstoffe DY-635 und DY-647 in biomimetischen und biologischen Modellsystemen untersucht. Zur Charakterisierung wurden dabei neben der Absorptionsspektroskopie insbesondere fluoreszenzspektroskopische Methoden verwendet. Dazu zählen die zeitkorrelierte Einzelphotonenzählung zur Ermittlung des Fluoreszenzabklingverhaltens, Fluoreszenz-Korrelations-Spektroskopie (FCS) zur Beobachtung von Diffusions- und photophysikalischen Desaktivierungsprozessen und die zeitaufgelöste Fluoreszenzanisotropie zur Untersuchung der Rotationsdynamik und Beweglichkeit der Farbstoffe im jeweiligen Modellsystem. Das Biotin-Streptavidin-System wurde als Modellsystem für die Untersuchung von Protein-Ligand-Wechselwirkungen verwendet, da der Bindungsmechanismus weitgehend aufgeklärt ist. Nach Bindung der Farbstoffe an Streptavidin wurde eine erhebliche Veränderung in den Absorptions- und Fluoreszenzeigenschaften beobachtet. Es wird angenommen, dass diese spektralen Veränderungen durch Wechselwirkung von benachbarten, an ein Streptavidintetramer gebundenen Farbstoffmolekülen und Bildung von H-Dimeren verursacht wird. Für das System Biotin-Streptavidin ist bekannt, dass während der Bindung des Liganden (Biotin) an das Protein eine Konformationsänderung auftritt. Anhand von zeitaufgelösten Fluoreszenzanisotropieuntersuchungen konnte in dieser Arbeit gezeigt werden, dass diese strukturellen Veränderungen zu einer starken Einschränkung der Beweglichkeit des Farbstoffes DY-635B führen. Liegt eine Mischung von ungebundenem und Streptavidin-gebundenem Farbstoff vor, können die Anisotropieabklingkurven nicht nach einem exponentiellen Verlauf angepasst werden. Es konnte im Rahmen dieser Arbeit gezeigt werden, dass in diesem Fall die Auswertung mit Hilfe des Assoziativen Anisotropiemodells möglich ist, welches eine Unterscheidung der Beiträge aus den zwei verschiedenen Mikroumgebungen ermöglicht. Als zweites Modellsystem dieser Arbeit wurden Mizellen des nichtionischen Tensids Tween-20 eingesetzt. Mizellen bilden eines der einfachsten Systeme, um die Mikroumgebung einer biologischen Membran nachzuahmen. Sind die Farbstoffe in den Mizellen eingelagert, so kommt es zu keiner Veränderung der Mizellgröße. Die ermittelten Werte des Diffusionskoeffizienten der mizellar eingelagerten Farbstoffe spiegeln demzufolge die Translationsbewegung der Tween-20-Mizellen wider. Die Beweglichkeit der Farbstoffe innerhalb der Tween-20-Mizellen wurde durch zeitaufgelöste Fluoreszenzanisotropiemessungen untersucht. Neben der „Wackelbewegung“, entsprechend dem wobble-in-a-cone-Modell, wird zusätzlich noch die laterale Diffusion der Farbstoffe entlang der Mizelloberfläche beschrieben.
To investigate processes in biological systems on a molecular level, particularly fluorescence spectroscopic methods have proven. The possibility to observe single molecules led to significant progress in the understanding of basic biochemical processes. Fluorescence correlation spectroscopy (FCS) is one of the most popular methods of single molecule spectroscopy and is a powerful technique for the investigation of intramolecular and diffusion-controlled processes on a µs to ms time scale. The photophysical characteristics of fluorescent probes are often strongly influenced by their microenvironment. For confocal microscopy and single molecule detection applications fluorescent dyes with properties, such as high photostability and high fluorescence efficiency are highly needed. Due to the high fluorescence efficiency and the high potential to design tailor-made fluorescence probes covering a wide spectral range in absorption and fluorescence, cyanine dyes are highly attractive as fluorescence probes for bioanalytical applications, such as clinical diagnostics and life sciences. The dyes DY-635 and DY-647 are two typical representatives of this class of dyes and can be covalently attached to biologically relevant molecules. Because of their excitation wavelength above 630nm these dyes are especially suited for bioanalytical applications. In this work the spectroscopic properties of DY-635 and DY-647 in biomimetic and biological model systems were studied by absorption and fluorescence spectroscopy techniques: time-correlated single photon counting to determine fluorescence decay behavior, fluorescence correlation spectroscopy (FCS) to observe diffusion and photophysical deactivation processes, and fluorescence anisotropy to study the mobility and rotational behavior of the dyes in the respective model system. The well characterized system biotin-streptavidin was used as a model system for protein-ligand interactions. Binding to streptavidin resulted in significant changes in the steady-state photophysical characteristics of DY-635B and DY-647. These spectral changes are attributed to dye-dye interactions and the formation of H-dimers. Previous studies have demonstrated, that binding of biotin alters the conformation of streptavidin. Based on the evaluation of time-resolved anisotropy data in this study it was shown that these structural changes result in strong hindrance of the rotational freedom of DY-635B. For mixtures of unbound and streptavidin-bound dyes the fluorescence anisotropy decay curves are found to be nonexponential. In this case the concept of an associated anisotropy were applied which allowed discrimination between contributions from different microenvironments. As a second model system, micelles of the nonionic surfactant Tween-20 were used. Micelles are one of the simplest systems to mimic the microenvironment of a biological membrane. Incorporation of the dyes had no effect on the micelle size. The diffusion coefficient of the dyes, obtained by fluorescence correlation spectroscopy (FCS), reflects the translational behavior of Tween-20 micelles. The mobility of the dyes in the Tween-20 micelles was studied by time-resolved fluorescence anisotropy. In addition to a „wobbling“ motion ccording to the wobble-in-a-cone model, a lateral diffusion of the dyes along the micelle surface is described.

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Stephan, Milena. "Development of a Biomembrane Sensor Based on Reflectometry." Doctoral thesis, Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2013. http://hdl.handle.net/11858/00-1735-0000-0001-BB7E-B.

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Membranproteine spielen eine wichtige Rolle in vielen biochemischen Prozessen der Zelle, wie zum Beispiel der Signaltransduktion, der Zelladhesion oder auch der Erkennung von Krankheitserregern. Viele dieser Proteine sind von Bedeutung für die Entwicklung neuer innovativer Medikamente. Somit hat auch die Entwicklung von Sensoren, die die Untersuchung von Membranproteinen in ihrer natürlichen Umgebung erlauben an Bedeutung gewonnen [1]. Thema dieser Doktorarbeit war die Entwicklung von Analysekonzepten die es ermöglichen unterschiedliche Aspekte von Membraninteraktionen zu untersuchen und zu quantifizieren. Als Analysemethode wurde dafür reflektometrische Interferenz Spektroskopie (RIfS) eine markierungsfreie, optische Methode verwendet. RIfS erlaubt es die Höhe dünner transparenter Filme zu bestimmen, indem das Weißlicht-Reflexionspektrum eines solchen Films aufgezeichnet wird. Durch die Überlagerung der in dem Film mehrfach reflektierten Teilstrahlen entsteht ein Interferenzmuster im Reflexionsspektrum, welches Aufschluß gibt über die Schichtdicke und den Brechungsindex des transparenten Films. Es wurde bereits gezeigt, dass RIfS eine geeignete Methode zur Untersuchung von Protein-ProteinWechselwirkungen ist [2]. Aus diesem Grund wurde RIfS als Detektionsverfahren für die Entwicklung eines Membransensors gewählt. Im Laufe dieser Arbeit entstanden zwei Aufbauten für reflektometrische Messungen. Ein Standard RIfS Aufbau und ein Instrument das die Methode mit Fluoreszenz-Mikroskopie kombiniert. Um dieWechselwirkung von Proteinen selbst und Proteinen mit Membranbestandteilen wie Lipiden zu untersuchen, wurde ein Konzept basierend auf festkörperunterstützten Membranen entwickelt. Dieses Experiment erlaubt es die Wechselwirkungen auf artifiziellen Membranen, sowie auf rekonstituierten Zellmembranen zu untersuchen. Zudem wurde ein Analysekonzept mit Nano-BLMs entwickelt, dass es erlaubt den simultanen Transport von Molekülen in ein membranverschlossenes Kompartiment hinein als auch heraus zu beobachten. Neben diesen membranbasierten Experimenten wurde auch ein Konzept entwickelt, welches es erlaubt die molekulare Erkennungsreaktion von sehr kleiner Analyten direkt zu messen. Dieses Messkonzept erlaubt es die Bindung von Molekülen mit sehr kleinem Molekulargewicht an einen auf dem Sensor immobilisierten Partner direkt zu quantifizieren.

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Books on the topic "Biotin-Streptavidin"

1

Domingo, Rommel J. Pre-targeted radioimmunotherapy with streptavidin-CC49 monoclonal antibody and p9sp0sY-DOTA-biotin. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1999.

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Domingo, Rommel J. Pre-targeted radioimmunotherapy with streptavidin-cc49 monoclonal antibody and 90y-dota-biotin. 1997.

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3

1958-, McMahon Robert Joseph, ed. Avidin-biotin interactions: Methods and applications. Totowa, NJ: Humana, 2008.

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1958-, McMahon Robert Joseph, ed. Avidin-biotin interactions: Methods and applications. Totowa, NJ: Humana, 2008.

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Avidin-Biotin Interactions: Methods and Applications (Methods in Molecular Biology). Humana Press, 2008.

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Book chapters on the topic "Biotin-Streptavidin"

1

Stöcker, W., and W. Schlumberger. "Biotin-Streptavidin-Technik." In Springer Reference Medizin, 451–52. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_575.

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Stöcker, W., and W. Schlumberger. "Biotin-Streptavidin-Technik." In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49054-9_575-1.

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Windbacher, Thomas, Viktor Sverdlov, and Siegfried Selberherr. "Biotin-Streptavidin Sensitive BioFETs and Their Properties." In Biomedical Engineering Systems and Technologies, 85–95. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-11721-3_6.

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Ebner, Andreas, Markus Marek, Karl Kaiser, Gerald Kada, Christoph D. Hahn, Bernd Lackner, and Hermann J. Gruber. "Application of Biotin-4-Fluorescein in Homogeneous Fluorescence Assays for Avidin, Streptavidin, and Biotin or Biotin Derivatives." In Avidin-Biotin Interactions, 73–88. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-579-4_7.

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LaRochelle, William J. "Detection of Proteins on Blots Using Avidin- or Streptavidin-Biotin." In Springer Protocols Handbooks, 323–27. Totowa, NJ: Humana Press, 1996. http://dx.doi.org/10.1007/978-1-60327-259-9_49.

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Jin, Xuejiao, Xiuling Cao, and Beidong Liu. "Isolation of Aged Yeast Cells Using Biotin-Streptavidin Affinity Purification." In Methods in Molecular Biology, 223–28. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0868-5_17.

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Coene, Elisabeth D., Michael K. Shaw, and David J. Vaux. "Anti-Biotin Antibodies Offer Superior Organelle-Specific Labelling of Mitochondria Over Avidin or Streptavidin." In Avidin-Biotin Interactions, 157–70. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-579-4_14.

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Humbert, Nicolas, and Thomas R. Ward. "Functionality Screen of Streptavidin Mutants by Non-Denaturing SDS–PAGE Using Biotin-4-Fluorescein." In Avidin-Biotin Interactions, 63–71. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-579-4_6.

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Hou, Shuai, Lei Shi, and Haixin Lei. "Biotin–Streptavidin Affinity Purification of RNA–Protein Complexes Assembled In Vitro." In Methods in Molecular Biology, 23–34. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3591-8_3.

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Richardson, M. D., L. A. McTaggart, and G. S. Shankland. "A Rapid Double Antibody Biotin-Streptavidin Elisa for Aspergillus Fumigatus Glycoprotein Antigen." In Fungal Antigens, 386. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-0773-0_59.

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Conference papers on the topic "Biotin-Streptavidin"

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Heller, Michael J., Dieter Dehlinger, Sadik Esener, and Benjamin Sullivan. "Electric Field Directed Fabrication of Biosensor Devices From Biomolecule Derivatized Nanoparticles." In ASME 2007 2nd Frontiers in Biomedical Devices Conference. ASMEDC, 2007. http://dx.doi.org/10.1115/biomed2007-38093.

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An electronic microarray has been used to carry out directed self-assembly of higher order 3D structures from Biotin/Streptavidin and DNA derivatized nanoparticles. Structures with more than forty layers of alternating biotin and streptavidin and DNA nanoparticles were fabricated using a 400 site CMOS microarray system. In this process, reconfigurable electric fields produced by the microarray device have been used to rapidly transport, concentrate and accelerate the binding of 40 and 200 nanometer biotin, streptavidin, DNA and peroxidase derivatized nanoparticles to selected sites on the microarray. The nanoparticle layering process takes less than one minute per layer (10–20 seconds for addressing and binding nanoparticles, 40 seconds for washing). The nanoparticle addressing/binding process can be monitored by changes in fluorescence intensity as each nanoparticle layer is deposited. The final multilayered 3-D structures are about two microns in thickness and 50 microns in diameter. Work is now focused on assembling “micron size” biosensor devices from bio-molecule derivatized luminescent and fluorescent nanoparticles. The proposed structure for a nanolayered glucose sensor device includes a base layer of biotin/streptavidin nanoparticles, a layer of glucose oxidase derivatized nanoparticles, a layer of peroxidase derivatized nanoparticles, a layer of quantum dots, and a final layer of biotin/streptavidin nanoparticles. Such a device will serve as a prototype for a wide variety of applications which includes other biosensor devices, lab-on a-chip devices, in-vivo drug delivery systems and “micron size” dispersible bio/chem sensors for environmental, military and homeland security applications.

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Niether, Doreen, Mona Sarter, Bernd König, Michaela Zamponi, Jörg Fitter, Andreas Stadler, and Simone Wiegand. "Thermodiffusion as a probe of protein hydration for streptavidin and the streptavidin-biotin complex." In THE IRAGO CONFERENCE 2017: A 360-degree Outlook on Critical Scientific and Technological Challenges for a Sustainable Society. Author(s), 2018. http://dx.doi.org/10.1063/1.5021914.

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"STUDY OF THE PROPERTIES OF BIOTIN-STREPTAVIDIN SENSITIVE BIOFETS." In International Conference on Biomedical Electronics and Devices. SciTePress - Science and and Technology Publications, 2009. http://dx.doi.org/10.5220/0001430700240030.

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Porwal, Pratik, Azeemuddin Syed, Prabhakar Bhimalapuram, and Tapan Kumar Sau. "Detection of biotin-streptavidin interaction using RF interdigitated capacitive cavity." In 2016 IEEE MTT-S International Microwave and RF Conference (IMaRC). IEEE, 2016. http://dx.doi.org/10.1109/imarc.2016.7939624.

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Li, Qingbin, Sergey Gusarov, and Andriy Kovalenko. "Molecular Dynamics Study of Streptavidin Binding to Surface-Immobilized Biotin." In 2008 International Symposium on Computer Science and Computational Technology. IEEE, 2008. http://dx.doi.org/10.1109/iscsct.2008.375.

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Windbacher, Thomas, Viktor Sverdlov, Siegfried Selberherr, Clemens Heitzinger, Norbert Mauser, Christian Ringhofer, Marília Caldas, and Nelson Studart. "Simulation of Field-Effect Biosensors (BioFETs) for Biotin-Streptavidin Complexes." In PHYSICS OF SEMICONDUCTORS: 29th International Conference on the Physics of Semiconductors. AIP, 2010. http://dx.doi.org/10.1063/1.3295530.

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Dalir, Hamid, Roohollah Dermanaki Farahani, Martin Le´vesque, and Daniel Therriault. "UV-Assisted Direct-Write Assembly of Scaffold-Templated Nanoclay Composites via Biotin-Streptavidin Interactions." In ASME 2010 International Mechanical Engineering Congress and Exposition. ASMEDC, 2010. http://dx.doi.org/10.1115/imece2010-39103.

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Three-dimensional epoxy scaffolds with abundant active epoxy groups on surfaces were fabricated through UV-assisted direct-write manufacturing process. The prepared scaffolds composed of cylindrical filaments (diameter ∼100 μm) were aminated by reacting the epoxy groups with 1, 3-diaminopropane. The resulting aminated scaffolds were subsequently biotinylated and then successfully applied to immobilize biotinylated nanoclay conjugates via a specific, strong and rapid binding of biotin and streptavidin. In another approach, the same amount of nanoclays was properly dispersed in epoxy by three-roll mill machine inducing high shear mixing. The nanoclay-epoxy filaments were then deposited by a computerized-control robot in a 3D micro structure scaffold form. Tensile mechanical tests were performed with a dynamic mechanical analysis (DMA) using a film tension clamp on three microstructures: nanoclay-epoxy scaffolds, aminated-biotinylated nanoclays coated on unloaded epoxy scaffolds and finally unloaded epoxy scaffolds (used as a reference). DMA tensile measurements indicated a slight improvement in modulus (by ∼5%), but significant increase in strength (by ∼24%), fracture strain (by ∼21%) and fracture energy (by ∼38%) by introducing biotin-streptavidin strong bonds among epoxy scaffolds and nanoclays in comparison with those of mixed nanoclay-epoxy scaffolds. These mechanical improvements are attributed to the strong biotin and streptavidin bonds between the epoxy scaffolds and nanoclays.

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Chen, Hong, Assem Abolmaaty, Peng Li, Constantine Anagnostopoulos, Stefan Du¨bel, and Mohammad Faghri. "Heterogeneous Detection of PCR-Amplified Intimin Gene From E. Coli O157:H7 via PDMS Microfluidic Chip." In ASME 2009 International Mechanical Engineering Congress and Exposition. ASMEDC, 2009. http://dx.doi.org/10.1115/imece2009-11796.

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E. coli O157:H7 strains represent the most important group of food-borne pathogens. PCR-amplified intimin gene of pathogenic E. coli O157:H7 was detected heterogeneously via a microfluidic chip that consists of streptavidin-coated nanoliter chambers. Biotinylated primers and digoxigenin labeled deoxyuridine triphosphate (dUTP) were incorporated into the amplified intimin (eaeA) gene by an off-chip PCR thermal cycler. The amplified products were injected into the chip where they were immobilized via streptavidin-biotin interaction. Detection of the products using alkaline phosphatase (AP) conjugated anti-digoxigenin was performed with an epi-fluorescent microscope. This assay was capable of detecting 0.06 ng/μL biotin-digoxigenin-dsDNA conjugate distinctly, which is a hundred fold more sensitive than the traditional detection by agarose gel.

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Dif, A., S. Touchet, S. Nagarajan, M. Baudy-Floc'h, M. Dahan, J. Piehler, and V. Marchi-Artzner. "Bioactivation of water-soluble peptidic quantum dot through biotin-streptavidin binding." In Biomedical Optics (BiOS) 2008, edited by Marek Osinski, Thomas M. Jovin, and Kenji Yamamoto. SPIE, 2008. http://dx.doi.org/10.1117/12.764152.

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Sasso, Lawrence A., and Jeffrey D. Zahn. "Continuous Microfluidic Biosensing With Conjugated Paramagnetic Beads." In ASME 2008 International Mechanical Engineering Congress and Exposition. ASMEDC, 2008. http://dx.doi.org/10.1115/imece2008-67686.

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A microfluidic biosensing assay has been designed and tested with streptavidin coated paramagnetic microbeads and fluorescently conjugated biotin (Biotin-FITC). The device is a three-inlet, three-outlet channel made by soft lithography of polydimethylsiloxane (PDMS). A novel magnetic actuation scheme is used to manipulate the beads within the channel. The device has proven capable of measuring the antigen concentration of a continuous sample stream. It is proposed that this technology could be applied as a real-time immunosensing assay.

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Reports on the topic "Biotin-Streptavidin"

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Cantor, C. R. Radioimmunotargeting with modified streptavidin-biotin. Final report. Office of Scientific and Technical Information (OSTI), September 1998. http://dx.doi.org/10.2172/656479.

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