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Journal articles on the topic 'Biotin-Streptavidin'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

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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 (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 satura

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2

Stayton, Patrick S., Stefanie Freitag, Lisa A. Klumb, et al. "Streptavidin–biotin binding energetics." Biomolecular Engineering 16, no. 1-4 (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 (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 cont

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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 (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 300-960

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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 biot

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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 (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, 1

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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 (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 sequ

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8

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

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9

González, Martín, Luis A. Bagatolli, Izaskun Echabe, et al. "Interaction of Biotin with Streptavidin." Journal of Biological Chemistry 272, no. 17 (1997): 11288–94. http://dx.doi.org/10.1074/jbc.272.17.11288.

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10

Maeda, Yoshiaki, Tomoko Yoshino, Masaaki Takahashi, et al. "Noncovalent Immobilization of Streptavidin on In Vitro- and In Vivo-Biotinylated Bacterial Magnetic Particles." Applied and Environmental Microbiology 74, no. 16 (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

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11

Gitlin, G., E. A. Bayer, and M. Wilchek. "Studies on the biotin-binding sites of avidin and streptavidin. Tyrosine residues are involved in the binding site." Biochemical Journal 269, no. 2 (1990): 527–30. http://dx.doi.org/10.1042/bj2690527.

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The involvement of tyrosine in the biotin-binding sites of the egg-white glycoprotein avidin and the bacterial protein streptavidin was examined by using the tyrosine-specific reagent p-nitrobenzenesulphonyl fluoride (Nbs-F). Modification of an average of about 0.5 mol of tyrosine residue/mol of avidin subunit caused the complete loss of biotin binding. This indicates that the single tyrosine residue (Tyr-33) in the avidin subunit is directly involved in the biotin-binding site and that its modification by Nbs also abolishes the binding properties of a neighbouring subunit. This suggests that

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12

Piketty, Marie-Liesse, Dominique Prie, Frederic Sedel, et al. "High-dose biotin therapy leading to false biochemical endocrine profiles: validation of a simple method to overcome biotin interference." Clinical Chemistry and Laboratory Medicine (CCLM) 55, no. 6 (2017): 817–25. http://dx.doi.org/10.1515/cclm-2016-1183.

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Abstract Background: High-dose biotin therapy is beneficial in progressive multiple sclerosis (MS) and is expected to be adopted by a large number of patients. Biotin therapy leads to analytical interference in many immunoassays that utilize streptavidin-biotin capture techniques, yielding skewed results that can mimic various endocrine disorders. We aimed at exploring this interference, to be able to remove biotin and avoid misleading results. Methods: We measured free triiodothyronine (fT3), free thyroxine (fT4), thyroid-stimulating hormone (TSH), parathyroid homrone (PTH), 25-hydroxyvitamin

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13

Hsiao, Alexander P., and Michael J. Heller. "Electric-Field-Directed Self-Assembly of Active Enzyme-Nanoparticle Structures." Journal of Biomedicine and Biotechnology 2012 (2012): 1–9. http://dx.doi.org/10.1155/2012/178487.

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A method is presented for the electric-field-directed self-assembly of higher-order structures composed of alternating layers of biotin nanoparticles and streptavidin-/avidin-conjugated enzymes carried out on a microelectrode array device. Enzymes included in the study were glucose oxidase (GOx), horseradish peroxidase (HRP), and alkaline phosphatase (AP); all of which could be used to form a light-emitting microscale glucose sensor. Directed assembly included fabricating multilayer structures with 200 nm or 40 nm GOx-avidin-biotin nanoparticles, with AP-streptavidin-biotin nanoparticles, and

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14

Gitlin, G., I. Khait, E. A. Bayer, M. Wilchek, and K. A. Muszkat. "Studies on the biotin-binding sites of avidin and streptavidin. A chemically induced dynamic nuclear polarization investigation of the status of tyrosine residues." Biochemical Journal 259, no. 2 (1989): 493–98. http://dx.doi.org/10.1042/bj2590493.

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We applied the protein photochemically induced dynamic nuclear polarization (photo-c.i.d.n.p.) method to explore the conformation of the side chains of tyrosine, tryptophan and histidine residues in three biotin-binding proteins. The c.i.d.n.p. spectra of avidin, streptavidin and ‘core’ streptavidin were compared with those of their complexes with biotin and its derivatives. The data indicate that the single tyrosine residue (Tyr-33) of avidin is clearly inaccessible to the triplet flavin photo-c.i.d.n.p. probe. The same holds for all tryptophan and histidine side chains. Although the analogou

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15

LI, JINHUA, XIANZHONG YU, THOMAS E. WAGNER, and YANZHANG WEI. "A biotin-streptavidin-biotin bridge dramatically enhances cell fusion." Oncology Letters 8, no. 1 (2014): 198–202. http://dx.doi.org/10.3892/ol.2014.2067.

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16

Zotova, D. V., N. A. Grudinina, O. I. Antimonova, M. M. Shavlovsky, and D. S. Polyakov. "Localization and activity of recombinant streptavidin in cell fractions of Escherichia coli." Medical academic journal 18, no. 3 (2018): 69–76. http://dx.doi.org/10.17816/maj18369-76.

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The authors provide a genetic construct for obtaining recombinant biologically active wild type streptavidin with high yield. Addition of leader peptide and oligohistidine sequence to the streptavidin sequence makes it possible to isolate soluble streptavidin from the culture medium and from the soluble fraction. Temperature conditions for inducing of protein synthesis were found to have a significant effect on the distribution profile of streptavidin between fractions. The obtained protein product is not contaminated with endogenous biotin. The provided method excludes denaturation and renatu

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17

Jiang, Liping, Faying Li, Jinhui Feng, et al. "An optionality further amplification of an sandwich-type electrochemical immunosensor based on biotin–streptavidin–biotin strategy for detection of alpha fetoprotein." RSC Advances 6, no. 29 (2016): 24373–80. http://dx.doi.org/10.1039/c6ra01178k.

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18

Hollinshead, Michael, Jeremy Sanderson, and David J. Vaux. "Anti-biotin Antibodies Offer Superior Organelle-specific Labeling of Mitochondria over Avidin or Streptavidin." Journal of Histochemistry & Cytochemistry 45, no. 8 (1997): 1053–57. http://dx.doi.org/10.1177/002215549704500803.

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The mitochondrial matrix contains endogenously biotinylated proteins. These proteins can cause unexpected background signal when biotin–avidin- or biotin–streptavidin-based detection systems are used in immunocytochemistry. Here we show that this reactivity can be deliberately exploited, using a simple anti-biotin reagent, to obtain strong and highly specific labeling of mitochondria by both light and electron microscopy. The signal is substantially stronger than when either avidin or streptavidin is used to detect the endogenous biotin. These results confirm the accessibility of protein-bound

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19

Trambas, Christina, Zhong Lu, Tina Yen, and Ken Sikaris. "Depletion of biotin using streptavidin-coated microparticles: a validated solution to the problem of biotin interference in streptavidin–biotin immunoassays." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 55, no. 2 (2017): 216–26. http://dx.doi.org/10.1177/0004563217707783.

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Background Biotin interference in streptavidin-based immunoassays causes widespread analytical distortions that may lead to clinical confusion, inappropriate patient management and, ultimately, adverse events. Its prevalence has increased recently due to the increased use of high-dose biotin therapy in specific patient groups (notably multiple sclerosis) and possibly the general community. Methods We have developed a method to deplete biotin from samples using the streptavidin-coated magnetic microparticles that are a component of most susceptible assays. Results We show that high concentratio

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20

Mzougui, Samy, Julien Favresse, Reza Soleimani, Catherine Fillée, and Damien Gruson. "Biotin interference: evaluation of a new generation of electrochemiluminescent immunoassays for high-sensitive troponin T and thyroid-stimulating hormone testing." Clinical Chemistry and Laboratory Medicine (CCLM) 58, no. 12 (2020): 2037–45. http://dx.doi.org/10.1515/cclm-2020-0214.

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AbstractBackgroundBiotin is currently a matter of concern for laboratories using biotin-streptavidin-based immunoassays. Biotin interferences have been reported for high-sensitive troponin T (hsTnT) and thyroid-stimulating hormone (TSH) assays. We aimed to evaluate the new generation of hsTnT and TSH electrochemiluminescent immunoassays announced to be less sensitive to biotin.MethodsFirstly, we assessed the analytical performances of new generation assays (imprecision, bias, total error, limit of quantification) and compared previous and new generation assays in the absence of biotin. Secondl

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21

SCHNYDER, Anita, Stefan KRÄHENBÜHL, Michael TÖRÖK, Jürgen DREWE, and Jörg HUWYLER. "Targeting of skeletal muscle in vitro using biotinylated immunoliposomes." Biochemical Journal 377, no. 1 (2004): 61–67. http://dx.doi.org/10.1042/bj20031034.

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In the present study, a non-covalent (biotin–streptavidin) coupling procedure for the preparation of pegylated immunoliposomes is presented, which simplifies the attachment of targeting vectors to sterically stabilized liposomes. A biotinylated poly(ethylene glycol) (PEG)-phospholipid [bio-PEG-distearoylphosphatidylethanolamine (DSPE)] was used as a linker between a streptavidin-conjugated monoclonal antibody (mAb) (i.e. the OX26 mAb raised against the rat transferrin receptor) and 150 nm liposomes. OX26–streptavidin had a biotin binding capacity of two to three biotin molecules per OX26–strep

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22

Schendel, Leonard C., Steffen M. Sedlak, and Hermann E. Gaub. "Switchable reinforced streptavidin." Nanoscale 12, no. 12 (2020): 6803–9. http://dx.doi.org/10.1039/d0nr00265h.

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23

Frame, Ithiel J., Parag H. Joshi, Caroline Mwangi, et al. "Susceptibility of Cardiac Troponin Assays to Biotin Interference." American Journal of Clinical Pathology 151, no. 5 (2019): 486–93. http://dx.doi.org/10.1093/ajcp/aqy172.

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Abstract Objectives To investigate biotin interference on three cardiac troponin (cTn) assays and demonstrate a method to overcome biotin interference. Methods cTn levels were measured in (1) plasma from healthy volunteers on 10-mg daily biotin supplementation mixed with a plasma with known elevated troponin, (2) plasmas with known elevated cTn after mixing in reagent biotin to simulate supplementation, and (3) biotin-spiked plasma specimens pretreated with streptavidin-agarose beads. Results Daily biotin ingestion (10 mg) and studies simulating daily biotin use resulted in significant interfe

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24

Liao, Renjie, Thai Pham, Diego Mastroeni, Paul D. Coleman, Joshua Labaer, and Jia Guo. "Highly Sensitive and Multiplexed In-Situ Protein Profiling with Cleavable Fluorescent Streptavidin." Cells 9, no. 4 (2020): 852. http://dx.doi.org/10.3390/cells9040852.

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The ability to perform highly sensitive and multiplexed in-situ protein analysis is crucial to advance our understanding of normal physiology and disease pathogenesis. To achieve this goal, we here develop an approach using cleavable biotin-conjugated antibodies and cleavable fluorescent streptavidin (CFS). In this approach, protein targets are first recognized by the cleavable biotin-labeled antibodies. Subsequently, CFS is applied to stain the protein targets. Though layer-by-layer signal amplification using cleavable biotin-conjugated orthogonal antibodies and CSF, the protein detection sen

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25

Koo, Kai, Peggy M. Foegeding, and Harold E. Swaisgood. "Development of a Streptavidin-Conjugated Single-Chain Antibody That Binds Bacillus cereusSpores." Applied and Environmental Microbiology 64, no. 7 (1998): 2497–502. http://dx.doi.org/10.1128/aem.64.7.2497-2502.1998.

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ABSTRACT Control of microorganisms such as Bacillus cereusspores is critical to ensure the safety and a long shelf life of foods. A bifunctional single chain antibody has been developed for detection and binding of B. cereus T spores. The genes that encodeB. cereus T spore single-chain antibody and streptavidin were connected for use in immunoassays and immobilization of the recombinant antibodies. A truncated streptavidin, which is smaller than but has biotin binding ability similar to that of streptavidin, was used as the affinity domain because of its high and specific affinity with biotin.

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Bayer, E. A., H. Ben-Hur, Y. Hiller, and M. Wilchek. "Postsecretory modifications of streptavidin." Biochemical Journal 259, no. 2 (1989): 369–76. http://dx.doi.org/10.1042/bj2590369.

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Streptavidin, an extracellular biotin-binding protein from Streptomyces avidinii, exhibits a multiplicity in its electrophoretic mobility pattern which depends both upon the conditions for growth of the bacterium and upon the protocol used in the purification of the protein. The observed structural heterogeneity appears to reflect the action of two types of postsecretory molecular events: proteolytic digestion of the intact Mr-18,000 subunit to a minimal molecular size (approx. Mr 14,000), and aggregation of the native tetramer into higher-order oligomeric forms. The extent of subunit degradat

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Berghorn, K. A., J. H. Bonnett, and G. E. Hoffman. "cFos immunoreactivity is enhanced with biotin amplification." Journal of Histochemistry & Cytochemistry 42, no. 12 (1994): 1635–42. http://dx.doi.org/10.1177/42.12.7983364.

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Through modification of the protocol by Adams, we developed a biotin amplification procedure for immunofluorescence staining of immediate early gene proteins and also applied biotin amplification for metal enhancement of diaminobenzidine staining in an immunoperoxidase protocol. Commercially available anti-cFos antisera were used to compare conventional "Elite" avidin-biotin complex reactions with biotin amplification reactions (visualized with peroxidase staining or streptavidin-Texas Red fluorescence). Biotin amplification and peroxidase staining (with or without nickel salts) enabled detect

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28

Dadfar, Seyed Mohammad Mahdi, Sylwia Sekula-Neuner, Vanessa Trouillet, et al. "Evaluation of click chemistry microarrays for immunosensing of alpha-fetoprotein (AFP)." Beilstein Journal of Nanotechnology 10 (December 16, 2019): 2505–15. http://dx.doi.org/10.3762/bjnano.10.241.

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The level of cancer biomarkers in cells, tissues or body fluids can be used for the prediction of the presence of cancer or can even indicate the stage of the disease. Alpha-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 sensitive fluorescent immunosensor for AFP detection. Three types of functionalized glasses (dibenzocyclooctyne- (DBCO-),

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29

Santi, Nicolò, Louis C. Morrill, and Louis Y. P. Luk. "Streptavidin-Hosted Organocatalytic Aldol Addition." Molecules 25, no. 10 (2020): 2457. http://dx.doi.org/10.3390/molecules25102457.

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In this report, the streptavidin-biotin technology was applied to enable organocatalytic aldol addition. By attaching pyrrolidine to the valeric motif of biotin and introducing it to streptavidin (Sav), a protein-based organocatalytic system was created, and the aldol addition of acetone with p-nitrobenzaldehyde was tested. The conversion of substrate to product can be as high as 93%. Although the observed enantioselectivity was only moderate (33:67 er), further protein engineering efforts can be included to improve the selectivity. These results have proven the concept that Sav can be used to

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30

Sedlak, Steffen M., Leonard C. Schendel, Hermann E. Gaub, and Rafael C. Bernardi. "Streptavidin/biotin: Tethering geometry defines unbinding mechanics." Science Advances 6, no. 13 (2020): eaay5999. http://dx.doi.org/10.1126/sciadv.aay5999.

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Macromolecules tend to respond to applied forces in many different ways. Chemistry at high shear forces can be intriguing, with relatively soft bonds becoming very stiff in specific force-loading geometries. Largely used in bionanotechnology, an important case is the streptavidin (SA)/biotin interaction. Although SA’s four subunits have the same affinity, we find that the forces required to break the SA/biotin bond depend strongly on the attachment geometry. With AFM-based single-molecule force spectroscopy (SMFS), we measured unbinding forces of biotin from different SA subunits to range from

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Khosravi, M. J., and R. C. Morton. "Novel application of streptavidin-hapten derivatives as protein-tracer conjugate in competitive-type immunoassays involving biotinylated detection probes." Clinical Chemistry 37, no. 1 (1991): 58–63. http://dx.doi.org/10.1093/clinchem/37.1.58.

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Abstract To investigate the use of streptavidin-hapten derivatives as potential protein-tracer conjugates for competitive-type immunoassays, we labeled streptavidin with cortisol and compared biotin-binding activity of the conjugates with that of unlabeled streptavidin. In this model system, streptavidin labeled with one to approximately 17 cortisol molecules retained its capability to cross-link a biotinylated protein on microtiter wells to a biotin-based general detection reagent developed for time-resolved fluorometry. Compared with unlabeled streptavidin, there was no reduction in the bind

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Hamblett, Kevin J., Brian B. Kegley, Don K. Hamlin, et al. "A Streptavidin−Biotin Binding System That Minimizes Blocking by Endogenous Biotin." Bioconjugate Chemistry 13, no. 3 (2002): 588–98. http://dx.doi.org/10.1021/bc010087t.

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Waner, Mark J., and David P. Mascotti. "A simple spectrophotometric streptavidin–biotin binding assay utilizing biotin-4-fluorescein." Journal of Biochemical and Biophysical Methods 70, no. 6 (2008): 873–77. http://dx.doi.org/10.1016/j.jbbm.2007.06.001.

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Niether, Doreen, Mona Sarter, Bernd W. Koenig, Jörg Fitter, Andreas M. Stadler, and Simone Wiegand. "Thermophoresis: The Case of Streptavidin and Biotin." Polymers 12, no. 2 (2020): 376. http://dx.doi.org/10.3390/polym12020376.

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Thermophoretic behavior of a free protein changes upon ligand binding and gives access to information on the binding constants. The Soret effect has also been proven to be a promising tool to gain information on the hydration layer, as the temperature dependence of the thermodiffusion behavior is sensitive to solute–solvent interactions. In this work, we perform systematic thermophoretic measurements of the protein streptavidin (STV) and of the complex STV with biotin (B) using thermal diffusion forced Rayleigh scattering (TDFRS). Our experiments show that the temperature sensitivity of the So

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Jones, M. Lisa, and Gary P. Kurzban. "Noncooperativity of Biotin Binding to Tetrameric Streptavidin." Biochemistry 34, no. 37 (1995): 11750–56. http://dx.doi.org/10.1021/bi00037a012.

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Wu, Yung-Peng, Chee Ying Chew, Tian-Neng Li, et al. "Target-activated streptavidin–biotin controlled binding probe." Chemical Science 9, no. 3 (2018): 770–76. http://dx.doi.org/10.1039/c7sc04014h.

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The streptavidin–biotin controlled binding probe has several advantages for the detection of enzymes and reactive small molecules, such as minimal background, multiple signal amplification steps, and wide selection of the optimal dyes for detection.

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Galarreta, Betty C., Peter R. Norton, and François Lagugné-Labarthet. "SERS Detection of Streptavidin/Biotin Monolayer Assemblies†." Langmuir 27, no. 4 (2011): 1494–98. http://dx.doi.org/10.1021/la1047497.

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Xu, Dongdong, and Seraphine V. Wegner. "Multifunctional streptavidin–biotin conjugates with precise stoichiometries." Chemical Science 11, no. 17 (2020): 4422–29. http://dx.doi.org/10.1039/d0sc01589j.

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Multifunctional streptavidin-biotin conjugates with defined stoichiometry and number of open binding pockets provide molecularly precise alternatives to the statistical mixture of products that typically forms.

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Yang, Haoyue, and Toshiya Sakata. "Molecular-Charge-Contact-Based Ion-Sensitive Field-Effect Transistor Sensor in Microfluidic System for Protein Sensing." Sensors 19, no. 15 (2019): 3393. http://dx.doi.org/10.3390/s19153393.

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In this paper, we demonstrate the possibility of direct protein sensing beyond the Debye length limit using a molecular-charge-contact (MCC)-based ion-sensitive field-effect transistor (ISFET) sensor combined with a microfluidic device. Different from the MCC method previously reported, biotin-coated magnetic beads are set on the gate insulator of an ISFET using a button magnet before the injection of target molecules such as streptavidin. Then, the streptavidin—a biotin interaction, used as a model of antigen—antibody reaction is expected at the magnetic beads/gate insulator nanogap interface

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Qiu, X. Q., K. S. Jakes, P. K. Kienker, A. Finkelstein, and S. L. Slatin. "Major transmembrane movement associated with colicin Ia channel gating." Journal of General Physiology 107, no. 3 (1996): 313–28. http://dx.doi.org/10.1085/jgp.107.3.313.

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Colicin Ia, a bacterial protein toxin of 626 amino acid residues, forms voltage-dependent channels in planar lipid bilayer membranes. We have exploited the high affinity binding of streptavidin to biotin to map the topology of the channel-forming domain (roughly 175 residues of the COOH-terminal end) with respect to the membrane. That is, we have determined, for the channel's open and closed states, which parts of this domain are exposed to the aqueous solutions on either side of the membrane and which are inserted into the bilayer. This was done by biotinylating cysteine residues introduced b

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Avery, Gordon. "Biotin interference in immunoassay: a review for the laboratory scientist." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 56, no. 4 (2019): 424–30. http://dx.doi.org/10.1177/0004563219842231.

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The recent FDA Biotin (Vitamin B7): Safety Communication – May Interfere with Lab Tests and A statement from the ACB Scientific Committee regarding biotin/vitamin B7 interference in immunoassays have raised into the laboratory consciousness the need to understand and to manage the issues around biotin interference with some immunoassays and to provide education and advice to health-care providers. In patients who are prescribed biotin or take biotin supplements, biotin has the potential to cause falsely low or falsely high results in immunoassays using streptavidin–biotin binding as part of th

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Freitag, Stefanie, Isolde Le Trong, Lisa A. Klumb, Patrick S. Stayton, and Ronald E. Stenkamp. "Atomic resolution structure of biotin-free Tyr43Phe streptavidin: what is in the binding site?" Acta Crystallographica Section D Biological Crystallography 55, no. 6 (1999): 1118–26. http://dx.doi.org/10.1107/s0907444999002322.

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The streptavidin–biotin system is an example of a high-affinity protein–ligand pair (Ka ≃ 1013 mol−1). The thermodynamic and structural properties have been extensively studied as a model system for protein–ligand interactions. Here, the X-ray crystal structure of a streptavidin mutant of a residue hydrogen bonding to biotin [Tyr43Phe (Y43F)] is reported at atomic resolution (1.14 Å). The biotin-free structure was refined with anisotropic displacement parameters (using the SHELXL97 program package). The high-resolution data also allowed interpretation of side-chain and residue disorder in 41 r

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Chang, Yaw Jen. "Patterned ZnO Nanowires between Interdigitated Electrodes by Integrating Hydrothermal Approach with Photolithography Process." Materials Science Forum 990 (May 2020): 283–87. http://dx.doi.org/10.4028/www.scientific.net/msf.990.283.

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This paper presents a simple approach to selectively synthesize the ZnO nanowires between interdigitated electrodes by integrating the hydrothermal method with the photolithography process. The printed circuit board (PCB) was adopted as the substrate. Interdigitated electrodes were fabricated by etching the copper foil of PCB. Then, both the positive and negative photoresists were used to control the growth of nanowires through lift-off concept. No costly materials and expensive apparatuses are required. Biotin–streptavidin reaction was used as an example to examine this proposed device. When

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Saha, Sounik, Ritankar Majumdar, Akhtar Hussain, Rajan R. Dighe, and Akhil R. Chakravarty. "Biotin-conjugated tumour-targeting photocytotoxic iron(III) complexes." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 371, no. 1995 (2013): 20120190. http://dx.doi.org/10.1098/rsta.2012.0190.

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Iron(III) complexes [FeL(B)] ( 1 – 4 ) of a tetradentate phenolate-based ligand (H 3 L) and biotin-conjugated dipyridophenazine bases (B), viz. 7-aminodipyrido [3,2- a :2′,3′- c ]-phenazine (dppza in 1 ), ( N -dipyrido[3,2- a :2′,3′- c ]-phenazino)amidobiotin (dppzNB in 2 ), dipyrido [3,2- a :2′,3′- c ]-phenazine-11-carboxylic acid (dppzc in 3 ) and 2-((2-biotinamido)ethyl) amido-dipyrido[3,2- a :2′,3′- c ]-phenazine (dppzCB in 4 ) are prepared, characterized and their interaction with streptavidin and DNA and their photocytotoxicity and cellular uptake in various cells studied. The high-spin

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Moore, Nathan W., Anthony R. C. Delacruz, Katherine S. Lancaster, Thorsten Dieckmann, and Tonya L. Kuhl. "Synthesis of a Reversible Streptavidin Binder for Biomimetic Assemblies." Australian Journal of Chemistry 60, no. 5 (2007): 363. http://dx.doi.org/10.1071/ch06319.

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The biotin/streptavidin ligand/receptor pair is used extensively in biotechnology. However, less is known about HABA (2-(4-hydroxyphenylazo)benzoic acid), which binds to streptavidin with a bond energy and dissociation constant that more closely mimics antibody/antigen interactions. In this work we demonstrate some of HABA’s useful properties that may make it a good substitute for biotin in a broad range of biochemical research. Specifically, we investigate its ease of conjugation to an anchoring pegylated lipid, characterization with MALDI, NMR, and visible-wavelength spectroscopies, and inco

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Ying, Le, Nuli Xie, Yanjing Yang, et al. "A cell-surface-anchored ratiometric i-motif sensor for extracellular pH detection." Chemical Communications 52, no. 50 (2016): 7818–21. http://dx.doi.org/10.1039/c6cc03163c.

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Ahlers, M., S. A. Darst, D. W. Grainger, et al. "Interaction of Proteins with Functional Monolayers: Recognition, 2D-Crystallization and Function." Proceedings, annual meeting, Electron Microscopy Society of America 48, no. 1 (1990): 608–9. http://dx.doi.org/10.1017/s0424820100181804.

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The interaction of molecular self organization and molecular recognition leads to the formation of functional supramolecular systems (see Figure 1). They combine order and mobility and their function is based on their organization.’ These fascinating phenomena - and the living cell is only the most perfect example - can help to mimic biomembrane processes as well as to develop new materials. The interaction of proteins with biomembranes is of fundamental relevance in many fields of biochemistry and medicine. Model biomembranes offer the possibility to simulate such naturally occuring processes

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Mondarte, Evan Angelo, Tatsuhiro Maekawa, Takashi Nyu, Hiroyuki Tahara, Ganchimeg Lkhamsuren, and Tomohiro Hayashi. "Detection of streptavidin–biotin intermediate metastable states at the single-molecule level using high temporal-resolution atomic force microscopy." RSC Advances 9, no. 39 (2019): 22705–12. http://dx.doi.org/10.1039/c9ra04106k.

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Han, Dong, Baolin Zhang, Chuangang Chong, Cuiping Rong, Jie Tan, and Rusen Yang. "A strategy for iron oxide nanoparticles to adhere to the neuronal membrane in the substantia nigra of mice." Journal of Materials Chemistry B 8, no. 4 (2020): 758–66. http://dx.doi.org/10.1039/c9tb02066g.

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Udompholkul, Parima, Carlo Baggio, Luca Gambini, et al. "Effective Tumor Targeting by EphA2-Agonist-Biotin-Streptavidin Conjugates." Molecules 26, no. 12 (2021): 3687. http://dx.doi.org/10.3390/molecules26123687.

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We recently reported on a potent synthetic agent, 135H11, that selectively targets the receptor tyrosine kinase, EphA2. While 135H11 possesses a relatively high binding affinity for the ligand-binding domain of EphA2 (Kd~130 nM), receptor activation in the cell required the synthesis of dimeric versions of such agent (namely 135H12). This was expected given that the natural ephrin ligands also need to be dimerized or clustered to elicit agonistic activity in cell. In the present report we investigated whether the agonistic activity of 135H11 could be enhanced by biotin conjugation followed by

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