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New Publication: TR-FRET Assay for UDP-Glycosyltransferases

by Hannah Lucas / Thursday, 26 May 2016 / Published in News

See our latest publication, “Development and Validation of a Universal High-Throughput UDP-Glycosyltransferase Assay with a Time-Resolved FRET Signal” in ASSAY and Drug Development Technologies


udp_glycotransferase_publication_graphic

BellBrook Labs scientist Tom Zielinski collaborated with investigators in Mel Reichman and Preston Donover of the Lankenau Institute for Medical Research to develop a robust assay method for screening and profiling glycosyltransferases, which are increasingly being targeted for metabolic diseases and cancer.

Abstract:

Glycosyltransferase enzymes play diverse metabolic and regulatory roles by catalyzing the transfer of sugarmolecules to protein, lipid, and carbohydrate acceptors, and they are increasingly of interest as therapeutic targets in a number of diseases, including metabolic disorders, cancer, and infectious diseases. The glycosyltransferases are a challenging target class from an assay development perspective because of the diversity of both donor and acceptor substrates and the lack of suitable glycan detection methods. However, many glycosyltransferases use uridine 50-diphosphate (UDP) sugars as donor substrates, and detection of the free UDP reaction product provides a generic approach for measuring the activity of those enzymes. To exploit this approach for a broadly applicable high-throughput screening (HTS) assay for discovery of glycosyltransferase inhibitors, we developed a Transcreener assay for immunodetection ofUDP with a time-resolved Fo¨rster resonance energy transfer (TR-FRET) signal.We optimized the assay for detection of glycosyltransferase activity with nucleotide diphosphate (NDP) sugars at concentrations from 10 lMto 1mM, achieving Z’ values of 0.6 or higher. The assay was validated by orthogonal pooled screeningwith 8,000 compounds using polypeptide N-acetylgalactosaminyltransferase T3 as the target, and the hits were confirmed using an orthogonal readout. The reagents and signal were both stable for more than 8 h at room temperature, insuring robust performance in automated HTS environments. The TR-FRET-based UDP detection assay provides a broadly applicable approach for screening glycosyltransferases that use a UDP-sugar donor.

 

Tagged under: Transcreener UDP Assay

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