A biotinylated peptide, BP21, alleviates hypotension in anaphylactic mice

2019 ◽  
Vol 25 (8) ◽  
Author(s):  
Akira Sato ◽  
Keiichi Ebina
Keyword(s):  
Biotinylated Peptide

Biotin–avidin interaction triggers conversion of triskelion peptide nanotori into nanochains

2018 ◽  
Vol 42 (5) ◽  
pp. 3452-3458 ◽  
Author(s):  
Vikas Kumar ◽  
Ramesh Singh ◽  
Khashti Ballabh Joshi
Keyword(s):  
Chain Formation ◽  
Self Assembled ◽  
Biotinylated Peptide

Triskelion biotinylated peptide is self-assembled into nanotorus structures followed by dimerization and chain formation in the presence of avidin.

Development of a Scintillation Proximity Assay for Histone Deacetylase Using a Biotinylated Peptide Derived from Histone-H4

1999 ◽  
Vol 267 (2) ◽  
pp. 390-396 ◽  
Author(s):  
Bakela Nare ◽  
John J. Allocco ◽  
Richard Kuningas ◽  
Stefan Galuska ◽  
Robert W. Myers ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Histone H4 ◽  
Scintillation Proximity Assay ◽  
Biotinylated Peptide

scholarly journals High Density Protein Kinase Assay With Subattomole Sensitivity

1998 ◽  
Vol 3 (1) ◽  
pp. 29-35 ◽  
Author(s):  
Allan Tereba
Keyword(s):  
Protein Kinase ◽  
Binding Capacity ◽  
High Capacity ◽  
Microtiter Plate ◽  
Kinase Assay ◽  
High Signal ◽  
Specific Substrate ◽  
Biotin Binding ◽  
Subsequent Capture ◽  
Biotinylated Peptide

A rapid assay system based on incorporation of [γ-32P]ATP into biotinylated peptide substrates and their subsequent capture onto a high capacity streptavidin-coated membrane, SAM2™, has been developed for the detection of protein kinases. The system uses prenumbered and partially cut membrane squares for analyzing a limited number of samples or can be formatted to analyze up to 1,536 samples per microtiter plate footprint of 7.0 cm X 10.6 cm. The high biotin-binding capacity and low background of the membrane allows the use of nearly saturating amounts of most substrates, giving this system very high signal-to-noise ratios at low enzyme concentrations. Using cAMP-dependent Protein Kinase A (PKA) as a model system, as little as 0.3 amol of purified enzyme in 0.2 μl can be detected with a linear response range of over 3 orders of magnitude. cAMP-dependent kinase activity can be measured directly in tissue extracts by using a specific substrate and harsh washing procedures to reduce nonspecific backgrounds from proteins phosphorylated by other kinases. For increased assay flexibility, results can be analyzed either by PhosphorImager™ quantitation or by scintillation counting.

Amplified voltammetric characterization of cleavage of the biotinylated peptide by BACE1 and screening of BACE1 inhibitors

2013 ◽  
Vol 50 ◽  
pp. 224-228 ◽  
Author(s):  
Xinyao Yi ◽  
Hongxing Han ◽  
Yu Zhang ◽  
Jianxiu Wang ◽  
Yi Zhang ◽  
...  
Keyword(s):  
Biotinylated Peptide

Development of a Versatile Platform for Nuclear Receptor Screening Using AlphaScreen™

2003 ◽  
Vol 8 (2) ◽  
pp. 191-197 ◽  
Author(s):  
Nathalie Rouleau ◽  
Sophie Turcotte ◽  
Marie-Hélène Mondou ◽  
Philippe Roby ◽  
Roger Bossé
Keyword(s):  
Consensus Sequence ◽  
Retinoic Acid Receptors ◽  
Sensitive Assay ◽  
Nanomolar Concentration ◽  
Lxxll Motif ◽  
Highly Sensitive ◽  
Dimerization Interface ◽  
Biotinylated Peptide ◽  
Efficient Screening ◽  
Nr Activity

The interaction between nuclear receptors (NRs) and their coactivators, a key step in transcription regulation, requires a short consensus sequence called the LXXLL motif found in the coactivators’ structure. Using the AlphaScreen™ technology, the authors have taken advantage of this receptor-coactivator interaction to develop a highly sensitive assay to identify and characterize compounds modulating NR activity. Estrogen and retinoic acid receptors were chosen as models to demonstrate the versatility of the AlphaScreen technology: (1) the assay can be designed using different antibodies to capture either full-length receptors or receptor domains that have been tagged, (2) the assay can differentiate between ligands that act as agonists or antagonists because only agonists will allow recruitment of the coactivator sequence–derived peptide, and (3) the assay gives the opportunity to screen for antagonists targeting the ligand-binding site or the dimerization interface between the receptor and the coactivator. Titration of the receptor and biotinylated peptide indicates that AlphaScreen is highly sensitive, requiring nanomolar concentration of reagents. Competition isotherms performed with known receptor antagonists demonstrate that the assay is a useful tool to rank the antagonists according to their order of potency. Overall, the results presented here indicate that the versatility, sensitivity, robustness, and ease of execution of the AlphaScreen NR assay will allow for efficient screening of NR modulators. ( Journal of Biomolecular Screening 2003:191-197)

Development of a Scintillation Proximity Assay for Calcineurin Phosphatase Activity

1997 ◽  
Vol 2 (1) ◽  
pp. 19-23 ◽  
Author(s):  
Elaine Sullivan ◽  
Paul Hemsley ◽  
Anne Pickard
Keyword(s):  
Cyclic Adenosine Monophosphate ◽  
Adenosine Monophosphate ◽  
Regulatory Subunit ◽  
Dependent Protein Kinase ◽  
Scintillation Proximity Assay ◽  
Large Numbers ◽  
Dependent Protein ◽  
Biotinylated Peptide ◽  
Calcineurin Phosphatase ◽  
Calcineurin Activity

We have developed a scintillation proximity assay (SPA) that allows the Ca2+/calmodulin (CaM)-dependent Serine/threoine (Ser/Thr) phosphoprotein phosphatase 2B (calcineurin) activity to be analyzed. A [33P] labeled and biotinylated peptide containing a partial sequence of the regulatory subunit (Rn) of the cyclic adenosine monophosphate (cAMP)-dependent protein kinase was synthesized and used as a synthetic substrate for calcineurin. Following incubation of the peptide with calcineurin, which removes the [33P] label, streptavidin-coated SPA beads were added to capture the biotinylated peptide (the level of the signal detected is inversely proportional to that of the calcineurin activity). Sensitivity is increased in this system by settling or centrifuging the streptavidin-coated SPA beads after binding has occurred. This method allows calcineurin phosphatase assays to be carried out in a 96-well format that is amenable to screening large numbers of compounds.

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