High-Throughput Screening of Selectivity of Melt Polymerization Catalysts Using Fluorescence Spectroscopy and Two-Wavelength Fluorescence Imaging

2003 ◽  
Vol 75 (17) ◽  
pp. 4676-4681 ◽  
Author(s):  
Radislav A. Potyrailo ◽  
John P. Lemmon ◽  
Terry K. Leib
2016 ◽  
Vol 52 (14) ◽  
pp. 2944-2947 ◽  
Author(s):  
Liping Wang ◽  
Jianchao Lee ◽  
Meijuan Zhang ◽  
Qiannan Duan ◽  
Jiarui Zhang ◽  
...  

A high-throughput screening (HTS) method based on fluorescence imaging (FI) was built and applied to evaluate the catalytic performance of selenides-modified TiO2. A catalyst library comprising 1405 catalysts was established using color ink-jet printing technology.


PLoS ONE ◽  
2013 ◽  
Vol 8 (12) ◽  
pp. e82693 ◽  
Author(s):  
Fuun Kawano ◽  
Yuki Aono ◽  
Hideyuki Suzuki ◽  
Moritoshi Sato

2010 ◽  
Vol 352 (1-2) ◽  
pp. 140-146 ◽  
Author(s):  
Arnout F. Gerritsen ◽  
Martijn Bosch ◽  
Michel de Weers ◽  
Jan G.J. van de Winkel ◽  
Paul W.H.I. Parren

2021 ◽  
Author(s):  
Fenli Liu ◽  
Sifan Bi ◽  
Wenjing Wang ◽  
Qiannan Duan ◽  
Yunjin Feng ◽  
...  

In this study, we present a new fluorescence imaging-based high-throughput screening method to evaluate the catalytic performance of the polymetallic sulfide complex g-C3N4. In order to obtain a large number...


ChemCatChem ◽  
2015 ◽  
Vol 7 (23) ◽  
pp. 3978-3984 ◽  
Author(s):  
Meijuan Zhang ◽  
Jianchao Lee ◽  
Liping Wang ◽  
Qianlan Duan ◽  
Jiarui Zhang ◽  
...  

2015 ◽  
Vol 21 (1) ◽  
pp. 12-23 ◽  
Author(s):  
Thilo Riedl ◽  
Egon van Boxtel ◽  
Martijn Bosch ◽  
Paul W. H. I. Parren ◽  
Arnout F. Gerritsen

Antibody-drug conjugates (ADCs) represent a rapidly growing class of biotherapeutics that deliver drugs specifically to target cells by binding of the antibody component to surface receptors. The majority of ADCs require receptor internalization depending on intrinsic features of the specific ADC-antigen interaction. The development of potent ADCs would greatly benefit from the identification of efficiently internalizing antibodies at early stages of discovery. We developed a highly sensitive and rapid antibody internalization assay using an indirect Cypher5E label. The pH-activated CypHer5E label becomes fluorescent upon internalization into the acidic environment of endocytic organelles, whereas background fluorescence of noninternalized CypHer5E is minimal. The pH-dependency of the CypHer5E signal enables robust discrimination of antibody internalization from surface binding. The favorable signal-over-background ratio allows a homogeneous assay design with high-throughput fluorescence imaging in 384- and 1536-well formats. The biophysical readout of the primary internalization event substantially shortens incubation times compared to killing assays using toxin internalization. The assay was validated with tumor-relevant targets, including receptor tyrosine kinases (EGFR and HER2) and a class II cytokine receptor (TF) expressed by A431, AU565, and SKOV-3 cells and transient expression systems (CHO-S). Our method enables functional screening of large antibody libraries to identify therapeutic antibody candidates with internalization characteristics favorable for the development of ADCs.


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