A Streptavidin Surface on Planar Glass Substrates for the Detection of Biomolecular Interaction

Birkert, Oliver; Haake, Hans-Martin; Schütz, Armin; Mack, Jürgen; Brecht, Andreas; Jung, Günther; Gauglitz, Günter

doi:10.1006/abio.2000.4615

Cited by 47 publications

(19 citation statements)

References 29 publications

(27 reference statements)

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“…RIfS transducers were modified with two layers of polymer (diaminopolyethylene glycol (mean molecular mass of 2 kDa; Rapp Polymere, Tü bingen, Germany), as described (25) and subsequent immobilization of aminodextran (100 kDa) (Innovent, Jena, Germany) to reduce nonspecific binding of sample components to the sensor and provide binding sites for the diethylstilbestrol-derivative. Carboxyl groups were introduced by letting the sensor react with glutaric anhydride (SigmaAldrich, Deisenhofen, Germany) at 70 C for 2 h (26).…”

Section: Receptor Binding Assaysmentioning

confidence: 99%

Diet-Derived Polyphenol Metabolite Enterolactone Is a Tissue-Specific Estrogen Receptor Activator

et al. 2007

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Numerous dietary compounds can modify gene expression by binding to the members of the nuclear receptor superfamily of transcription factors. For example, dietary polyphenols, such as soy isoflavones genistein and daidzein, modulate the activity of the estrogen receptors (ERs)-alpha and ERbeta. An additional class of dietary polyphenols that modulate cellular signaling pathways are lignans, compounds that are common constituents of Western diets. In this study, we show that a metabolite of dietary lignans, enterolactone, at physiological concentrations, activates ER-mediated transcription in vitro with preference for ERalpha. The effects of enterolactone are mediated by the ER ligand binding domain and are susceptible to antiestrogen treatment. Furthermore, the affinity of enterolactone toward ERalpha, measured by a novel ligand binding assay, is augmented in cell culture conditions. Moreover, our results demonstrate for the first time that enterolactone has estrogenic activity in vivo. In transgenic estrogen-sensitive reporter mice, enterolactone induces tissue-specific estrogen-responsive reporter gene expression as well as promotes uterine stromal edema and expression of estrogen-responsive endogenous genes (CyclinD1 and Ki67). Taken together, our data show that enterolactone is a selective ER agonist inducing ER-mediated transcription both in vitro in different cell lines and in vivo in the mouse uterus.

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Section: Receptor Binding Assaysmentioning

confidence: 99%

Diet-Derived Polyphenol Metabolite Enterolactone Is a Tissue-Specific Estrogen Receptor Activator

et al. 2007

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“…[39,40] To prevent any nonspecific interactions on the electrode surface during measurement, PEG molecules known to inhibit nonspecific interactions were used as a spacer to immobilize the KIX peptide. [41] The degree of immobilization at each step was confirmed directly from frequency decreases (mass increases) by using the QCM in water.…”

Section: Preparation Of the Kid Peptidementioning

confidence: 99%

Kinetic Study of Phosphorylation‐Dependent Complex Formation between the Kinase‐Inducible Domain (KID) of CREB and the KIX Domain of CBP on a Quartz Crystal Microbalance

Matsuno

Furusawa

Okahata

2004

Chemistry A European J

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We report quantitative analysis of peptide-peptide interactions on a 27 MHz quartz crystal microbalance (QCM) in aqueous solution. The KID (kinase-inducible domain) of transcription factor CREB (cyclic AMP response element binding protein) is known to interact with the KIX domain of coactivator CBP (CREB binding protein), facilitated by phosphorylation at Ser-133 of the KID. The KIX domain peptide (86 aa) was immobilized on the QCM gold electrode surface by means of a poly(ethylene glycol) spacer. Binding of the KID peptide (46 aa) to the KIX peptide was detected by frequency decreases (mass increases) of the QCM. Both maximum binding amount (Deltammax) and association constants (Ka) obtained from the QCM measurements increased as a result of phosphorylation of Ser-133 of the KID peptide. The Ka values for KIX peptide to the phosphorylated (pKID) and unphosphorylated KID peptides were (93+/-2) x 10(3) and (5+/-1) x 10(3) M(-1), respectively. This difference was explained by the dissociation rate constant (k(-1)) of the pKID being 20 times smaller than that of the KID, while association rate constants (k1) were independent of phosphorylation.

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“…First, the interaction between biotin and SA is well-established and often serves as a model for immunoassays. [12] Second, the size of SA [13] matches the size of the Au nanoparticles used in this study. We thus expect the appropriate spacing (using matrix Al 2 O 3 as spacer) provide optimal space around each probe molecule for binding with SA, as well as an optimal density of probe molecules at the surface, leading to an enhanced response.…”

Section: Introductionmentioning

confidence: 99%

Highly Stable Au Nanoparticles with Tunable Spacing and Their Potential Application in Surface Plasmon Resonance Biosensors

Gao

Koshizaki

Tokuhisa

et al. 2009

Adv Funct Materials

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Colloidal Au‐amplified surface plasmon resonance (SPR), like traditional SPR, is typically used to detect binding events on a thin noble metal film. The two major concerns in developing colloidal Au‐amplified SPR lie in 1) the instability, manifested as a change in morphology following immersion in organic solvents and aqueous solutions, and 2) the uncontrollable interparticle distance, determining probe spacing and inducing steric hindrance between neighboring probe molecules. This may introduce uncertainties into such detecting techniques, degrade the sensitivity, and become the barricade hampering colloidal Au‐based transducers from applications in sensing. In this paper, colloidal Au‐amplified SPR transducers are produced by using ultrathin Au/Al2O3 nanocomposite films via a radio frequency magnetron co‐sputtering method. Deposited Au/Al2O3 nanocomposite films exhibit superior stability, and average interparticle distances between Au nanoparticles with similar average sizes can be tuned by changing surface coverage. These characteristics are ascribed to the spacer function and rim confinement of dielectric Al2O3 and highlight their advantages for application in optimal nanoparticle‐amplified SPR, especially when the probe size is smaller than the target molecule size. This importance is demonstrated here for the binding of protein (streptavidin) targets to the probe (biotin) surface. In this case, the dielectric matrix Al2O3 is a main contributor, behaving as a spacer, tuning the concentration of Au nanoparticles, and manipulating the average interparticle distance, and thus guaranteeing an appropriate number of biotin molecules and expected near‐field coupling to obtain optimal sensing performance.

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A Streptavidin Surface on Planar Glass Substrates for the Detection of Biomolecular Interaction

Cited by 47 publications

References 29 publications

Diet-Derived Polyphenol Metabolite Enterolactone Is a Tissue-Specific Estrogen Receptor Activator

Diet-Derived Polyphenol Metabolite Enterolactone Is a Tissue-Specific Estrogen Receptor Activator

Kinetic Study of Phosphorylation‐Dependent Complex Formation between the Kinase‐Inducible Domain (KID) of CREB and the KIX Domain of CBP on a Quartz Crystal Microbalance

Highly Stable Au Nanoparticles with Tunable Spacing and Their Potential Application in Surface Plasmon Resonance Biosensors

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