By Taosheng Chen
The improvement of appropriate assays, the combination of acceptable expertise, and the powerful administration of the basic infrastructure are all serious to the good fortune of any high-throughput screening (HTS) undertaking. even though, few scientists have the multidisciplinary adventure had to keep an eye on all elements of an HTS drug discovery venture. a realistic advisor to Assay improvement and High-Throughput Screening in Drug Discovery integrates the adventure of various specialists who provide primary and functional tips throughout quite a few occasions. The ebook first discusses assay advancements for very important goal sessions corresponding to protein kinases and phosphatases, proteases, nuclear receptors, G protein-coupled receptors, ion channels, and warmth surprise proteins. It subsequent examines assay advancements for mobilephone viability, apoptosis, and infectious ailments. The individuals discover the applying of rising applied sciences and platforms, together with image-based excessive content material screening, RNA interference, and first cells. eventually, they talk about the fundamental parts of the built-in HTS method, similar to screening automation, compound library administration, the screening of typical items from botanical assets, and screening informatics. Designed to encourage researchers to convey extra advances to the sphere, this quantity presents useful assistance on how one can start up, validate, optimize, and deal with a bioassay meant to display huge collections of compounds. Drawing at the wisdom from specialists actively interested by assay improvement and HTS, this can be a source that's either finished and centred.
Read or Download A Practical Guide to Assay Development and High-Throughput Screening in Drug Discovery (Critical Reviews in Combinatorial Chemistry) PDF
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Extra resources for A Practical Guide to Assay Development and High-Throughput Screening in Drug Discovery (Critical Reviews in Combinatorial Chemistry)
K. Shoichet. 2006. A detergent-based assay for the detection of promiscuous inhibitors. Nat. Protoc. 1, 550–553. F. and S. Ferrand. 2008. Scintillation proximity assays in high-throughput screening. Assay Drug Dev. Technol. 6, 433–455. F. et al. 2002. A comparison of AlphaScreen, TR-FRET, and TRF as assay methods for FXR nuclear receptors. J. Biomol. Screen. 7, 3–10. F. and A. Schmid. 2007. Farnesyl pyrophosphate synthase: real-time kinetics and inhibition by nitrogen-containing bisphosphonates in a scintillation assay.
Mass spectrometry is often useful for this purpose. Post-translational modifications or sequence truncations can potentially alter the compound binding sites available and can also change the structure of potential inhibitory sites. For example, with protein kinases, phosphorylations distal from the ATP binding site can inactivate the kinase whereas phosphorylations near the ATP binding site can activate the catalytic activity. Often, practice does not permit control of such situations because the purified systems are often mixtures and cannot be controlled in the commonly used recombinant expression technologies.
2006. Principles of Fluorescence Spectroscopy. 3rd ed. Berlin: Springer. S. and Q. Wang. 2007. Seeing is believing: peptide-based fluorescent sensors of protein tyrosine kinase activity. Chem. BioChem. 8, 373–378. F. Y. Zhang. 2001. Assays for protein-tyrosine phosphatases. Meth. Enzymol. 345, 507–518. K. 2003. Assays to measure the activation of membrane tyrosine kinase receptors: focus on cellular methods. Curr. Opin. Drug Discov. Devel. 6, 760–765. I. P. Kennedy. 2005. Protein tyrosine phosphatase: enzymatic assays.
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