scholarly journals Two-Photon Excitation in Fluorescence Polarization Receptor-Ligand Binding Assay

2005 ◽  
Vol 10 (4) ◽  
pp. 314-319 ◽  
Author(s):  
Marko E. Tirri ◽  
Roope J. Huttunen ◽  
Juha Toivonen ◽  
Pirkko L. Härkönen ◽  
Juhani T. Soini ◽  
...  

Fluorescence polarization is one of the most commonly used homogeneous assay principles in drug discovery for screening of potential lead compounds. In this article, the fluorescence polarization technique is combined with 2-photon excitation of fluorescence. Theoretically, the use of 2-photon excitation of fluorescence increases the volumetric sensitivity and polarization contrast of fluorescence polarization assays. The work in this report demonstrates these predictions for an estrogen receptor ligand binding assay.

2009 ◽  
Vol 392 (2) ◽  
pp. 103-109 ◽  
Author(s):  
Eija Martikkala ◽  
Mirva Lehmusto ◽  
Minna Lilja ◽  
Anita Rozwandowicz-Jansen ◽  
Jenni Lunden ◽  
...  

BIO-PROTOCOL ◽  
2015 ◽  
Vol 5 (6) ◽  
Author(s):  
Mari Wildhagen ◽  
Melinka Butenko ◽  
Reidunn Aalen ◽  
Georg Felix ◽  
Markus Albert

2008 ◽  
Vol 1094 ◽  
Author(s):  
Tomoko Yoshino ◽  
Chihiro Kaji ◽  
Tadashi Matsunaga

AbstractMagnetic particles are used for various biomedical applications because they are easy to both handle and separate from biological samples. Nano-sized bacterial magnetic particles (BacMPs) that display the human estrogen receptor ligand binding domain (ERLBD) on their surfaces were successfully produced by the magnetotactic bacterium,Magnetospirillum magneticumAMB-1. A receptor assay for endocrine-disrupting chemicals using ERLBD-displaying BacMPs was developed. A BacMP membrane-specific protein, Mms16 or Mms13, was used as an anchor protein to localize the ERLBD on the surfaces of BacMPs. ERLBD-BacMP complexes were assayed for competitive binding of alkaline phosphatase-conjugated 17β-estradiol (ALP-E2). Inhibition curve of ALP-E2 to the powerful antagonist, tamoxifen was generated by measuring decreases in luminescence intensity that resulted from the enzymatic reaction of alkaline phosphatase. The overall simplicity of this receptor-binding assay results in a method that can be easily adapted to a high-throughput format.


1975 ◽  
Vol 80 (1_Suppla) ◽  
pp. S15
Author(s):  
K. H. Rudorff ◽  
H. J. Kröll ◽  
J. Herrmann

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