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Journal articles on the topic 'Thermal shift assay'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 March 2023

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1

McMahon, Róisín M., Martin J. Scanlon, and Jennifer L. Martin. "Interrogating Fragments Using a Protein Thermal Shift Assay." Australian Journal of Chemistry 66, no. 12 (2013): 1502. http://dx.doi.org/10.1071/ch13279.

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Protein thermal shift is a relatively rapid and inexpensive technique for the identification of low molecular weight compound interactions with protein targets. An increase in the melting temperature of the target protein in the presence of a test ligand is indicative of a promising ligand–protein interaction. Due to its simplicity, protein thermal shift is an attractive method for screening libraries and validating hits in drug discovery programs. The methodology has been used successfully in high throughput screens of small molecule libraries, and its application has been extended to report

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2

DeLeeuw, Lynn W., Robert C. Monsen, Vytautas Petrauskas, et al. "POT1 stability and binding measured by fluorescence thermal shift assays." PLOS ONE 16, no. 3 (2021): e0245675. http://dx.doi.org/10.1371/journal.pone.0245675.

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The protein POT1 (Protection of Telomeres 1) is an integral part of the shelterin complex that protects the ends of human chromosomes from degradation or end fusions. It is the only component of shelterin that binds single-stranded DNA. We describe here the application of two separate fluorescent thermal shift assays (FTSA) that provide quantitative biophysical characterization of POT1 stability and its interactions. The first assay uses Sypro Orange™ and monitors the thermal stability of POT1 and its binding under a variety of conditions. This assay is useful for the quality control of POT1 p

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3

Dart, Melanie L., Thomas Machleidt, Emily Jost, et al. "Homogeneous Assay for Target Engagement Utilizing Bioluminescent Thermal Shift." ACS Medicinal Chemistry Letters 9, no. 6 (2018): 546–51. http://dx.doi.org/10.1021/acsmedchemlett.8b00081.

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4

Andreotti, Giuseppina, Maria Monticelli, and Maria Vittoria Cubellis. "Looking for protein stabilizing drugs with thermal shift assay." Drug Testing and Analysis 7, no. 9 (2015): 831–34. http://dx.doi.org/10.1002/dta.1798.

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5

YATA, YUYA, TAKAYUKI ISHIDA, MITSUTOSHI KUBOTA, TARO MASUDA, and HARUHIKO TOYOHARA. "Studies on the thermal denaturation of fish actomyosin by thermal shift assay." NIPPON SUISAN GAKKAISHI 80, no. 4 (2014): 594–600. http://dx.doi.org/10.2331/suisan.80.594.

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6

Fleischhauer, Lutz, Christoph Niemietz, Sara Reinartz Groba, et al. "Thermal shift assay for evaluation of transthyretin stability in plasma." Amyloid 24, sup1 (2017): 34–35. http://dx.doi.org/10.1080/13506129.2017.1281121.

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7

Kelm, Melanie, and Martin Knoll. "Real-Time-Erfassung der Proteinstabilität mit dem thermal shift assay." BIOspektrum 21, no. 1 (2015): 76–77. http://dx.doi.org/10.1007/s12268-015-0543-5.

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8

McMahon, Roisin M., Martin J. Scanlon, and Jennifer L. Martin. "ChemInform Abstract: Interrogating Fragments Using a Protein Thermal Shift Assay." ChemInform 45, no. 8 (2014): no. http://dx.doi.org/10.1002/chin.201408278.

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9

Pantoliano, Michael W., Eugene C. Petrella, Joseph D. Kwasnoski, et al. "High-Density Miniaturized Thermal Shift Assays as a General Strategy for Drug Discovery." Journal of Biomolecular Screening 6, no. 6 (2001): 429–40. http://dx.doi.org/10.1177/108705710100600609.

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More general and universally applicable drug discovery assay technologies are needed in order to keep pace with the recent advances in combinatorial chemistry and genomics-based target generation. Ligand-induced conformational stabilization of proteins is a well-understood phenomenon in which substrates, inhibitors, cofactors, and even other proteins provide enhanced stability to proteins on binding. This phenomenon is based on the energetic coupling of the ligand-binding and protein-melting reactions. In an attempt to harness these biophysical properties for drug discovery, fully automated in

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10

Kopra, Kari, Salla Valtonen, Randa Mahran, et al. "Thermal Shift Assay for Small GTPase Stability Screening: Evaluation and Suitability." International Journal of Molecular Sciences 23, no. 13 (2022): 7095. http://dx.doi.org/10.3390/ijms23137095.

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Thermal unfolding methods are commonly used as a predictive technique by tracking the protein’s physical properties. Inherent protein thermal stability and unfolding profiles of biotherapeutics can help to screen or study potential drugs and to find stabilizing or destabilizing conditions. Differential scanning calorimetry (DSC) is a ‘Gold Standard’ for thermal stability assays (TSA), but there are also a multitude of other methodologies, such as differential scanning fluorimetry (DSF). The use of an external probe increases the assay throughput, making it more suitable for screening studies,

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11

Teles, Andre Lacerda Braga, Roseane R. Silva, Michelle Ko, et al. "Identification, Characterization and Molecular Modelling Studies of Schistosoma mansoni Dihydrofolate Reductase Inhibitors: From Assay Development to Hit Identification." Current Topics in Medicinal Chemistry 18, no. 5 (2018): 406–17. http://dx.doi.org/10.2174/1568026618666180509150134.

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Introduction: Schistosoma mansoni is responsible for virtually all reported cases of schistosomiasis in Latin America and the emergence of praziquantel- and oxaminiquine-resistant strains makes it urgent to develop new schistosomicide agents. Dihydrofolate reductases (DHFR) from bacteria and protozoan parasites are considered validated macromolecular targets for this goal, but S. mansoni DHFR (SmDHFR) has been largely overlooked. To fill this gap in knowledge, the present work describes optimized conditions to carry out thermal shift assays with SmDHFR, as well as a balanced kinetic assay that

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12

Bhayani, Jaina A., and Miguel A. Ballicora. "Determination of dissociation constants of protein ligands by thermal shift assay." Biochemical and Biophysical Research Communications 590 (January 2022): 1–6. http://dx.doi.org/10.1016/j.bbrc.2021.12.041.

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13

Kroeger, Tobias, Benedikt Frieg, Tao Zhang, et al. "EDTA aggregates induce SYPRO orange-based fluorescence in thermal shift assay." PLOS ONE 12, no. 5 (2017): e0177024. http://dx.doi.org/10.1371/journal.pone.0177024.

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14

West, Graham M., J. Will Thompson, Erik J. Soderblom, et al. "Mass Spectrometry-Based Thermal Shift Assay for Protein−Ligand Binding Analysis." Analytical Chemistry 82, no. 13 (2010): 5573–81. http://dx.doi.org/10.1021/ac100465a.

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15

McNulty, Dean E., William G. Bonnette, Hongwei Qi, et al. "A High-Throughput Dose-Response Cellular Thermal Shift Assay for Rapid Screening of Drug Target Engagement in Living Cells, Exemplified Using SMYD3 and IDO1." SLAS DISCOVERY: Advancing the Science of Drug Discovery 23, no. 1 (2017): 34–46. http://dx.doi.org/10.1177/2472555217732014.

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A persistent problem in early small-molecule drug discovery is the frequent lack of rank-order correlation between biochemical potencies derived from initial screens using purified proteins and the diminished potency and efficacy observed in subsequent disease-relevant cellular phenotypic assays. The introduction of the cellular thermal shift assay (CETSA) has bridged this gap by enabling assessment of drug target engagement directly in live cells based on ligand-induced changes in protein thermal stability. Initial success in applying CETSA across multiple drug target classes motivated our in

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16

Owens, Ashley E., Michael J. Iannotti, Tino W. Sanchez, et al. "High-Throughput Cellular Thermal Shift Assay Using Acoustic Transfer of Protein Lysates." ACS Chemical Biology 17, no. 2 (2022): 322–30. http://dx.doi.org/10.1021/acschembio.1c00760.

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17

Jafari, Rozbeh, Helena Almqvist, Hanna Axelsson, et al. "The cellular thermal shift assay for evaluating drug target interactions in cells." Nature Protocols 9, no. 9 (2014): 2100–2122. http://dx.doi.org/10.1038/nprot.2014.138.

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18

McDonnell, Patricia A., Joseph Yanchunas, John A. Newitt, et al. "Assessing compound binding to the Eg5 motor domain using a thermal shift assay." Analytical Biochemistry 392, no. 1 (2009): 59–69. http://dx.doi.org/10.1016/j.ab.2009.05.044.

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19

Molina, Daniel Martinez, Rozbeh Jafari, Marina Ignatushchenko, et al. "Monitoring Drug Target Engagement in Cells and Tissues Using the Cellular Thermal Shift Assay." Science 341, no. 6141 (2013): 84–87. http://dx.doi.org/10.1126/science.1233606.

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The efficacy of therapeutics is dependent on a drug binding to its cognate target. Optimization of target engagement by drugs in cells is often challenging, because drug binding cannot be monitored inside cells. We have developed a method for evaluating drug binding to target proteins in cells and tissue samples. This cellular thermal shift assay (CETSA) is based on the biophysical principle of ligand-induced thermal stabilization of target proteins. Using this assay, we validated drug binding for a set of important clinical targets and monitored processes of drug transport and activation, off

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20

Lee, Po-Hsien, Xi Xiao Huang, Bin Tean Teh, and Ley-Moy Ng. "TSA-CRAFT: A Free Software for Automatic and Robust Thermal Shift Assay Data Analysis." SLAS DISCOVERY: Advancing the Science of Drug Discovery 24, no. 5 (2019): 606–12. http://dx.doi.org/10.1177/2472555218823547.

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Thermal shift assay (TSA) is an increasingly popular technique used for identifying protein stabilizing conditions or interacting ligands in X-ray crystallography and drug discovery applications. Although the setting up and running of TSA reactions is a relatively simple process, the subsequent analysis of TSA data, especially in high-throughput format, requires substantial amount of effort if conducted manually. We therefore developed the Thermal Shift Assay–Curve Rapid and Automatic Fitting Tool (TSA-CRAFT), a freely available software that enable automatic analysis of TSA data of any throug

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21

Zeis, Bettina, Jana Maurer, Olaf Pinkhaus, Eva Bongartz, and Rüdiger J. Paul. "A swimming activity assay shows that the thermal tolerance of Daphnia magna is influenced by temperature acclimation." Canadian Journal of Zoology 82, no. 10 (2004): 1605–13. http://dx.doi.org/10.1139/z04-141.

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Daphnia magna Straus, 1820 is a widespread zooplanktic organism enduring considerable changes in oxygen concentration and temperature within its natural habitat. The thermal tolerance window of D. magna was analyzed using the animals' swimming activity as a test parameter in a photometrical assay. Acclimation to different temperatures (10, 20, 30 °C) resulted in a shift of the thermal optimum corresponding to acclimation conditions. Acclimation to warm temperatures also increased the upper thermal tolerance limit in acute thermal tolerance tests. However, the magnitude of the resulting shift i

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22

Herledan, Adrien, Marine Andres, Aurore Lejeune-Dodge, et al. "Drug Target Engagement Using Coupled Cellular Thermal Shift Assay—Acoustic Reverse-Phase Protein Array." SLAS DISCOVERY: Advancing the Science of Drug Discovery 25, no. 2 (2019): 207–14. http://dx.doi.org/10.1177/2472555219897256.

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In the last 5 years, cellular thermal shift assay (CETSA), a technology based on ligand-induced changes in protein thermal stability, has been increasingly used in drug discovery to address the fundamental question of whether drug candidates engage their intended target in a biologically relevant setting. To analyze lysates from cells submitted to increasing temperature, the detection and quantification of the remaining soluble protein can be achieved using quantitative mass spectrometry, Western blotting, or AlphaScreen techniques. Still, these approaches can be time- and cell-consuming. To c

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23

Bhusal, Ram Prasad, Krunal Patel, Brooke X. C. Kwai, et al. "Development of NMR and thermal shift assays for the evaluation ofMycobacterium tuberculosisisocitrate lyase inhibitors." MedChemComm 8, no. 11 (2017): 2155–63. http://dx.doi.org/10.1039/c7md00456g.

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The enzymes isocitrate lyase (ICL) isoforms 1 and 2 are essential forMycobacterium tuberculosissurvival within macrophages during latent tuberculosis (TB). Herein we report the development of a combined NMR spectroscopy and thermal shift assay for the screening and evaluation of ICL inhibitors.

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24

Gradl, Stefan, Holger Steuber, Joerg Weiske, et al. "Discovery of the SMYD3 Inhibitor BAY-6035 Using Thermal Shift Assay (TSA)-Based High-Throughput Screening." SLAS DISCOVERY: Advancing the Science of Drug Discovery 26, no. 8 (2021): 947–60. http://dx.doi.org/10.1177/24725552211019409.

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SMYD3 (SET and MYND domain-containing protein 3) is a protein lysine methyltransferase that was initially described as an H3K4 methyltransferase involved in transcriptional regulation. SMYD3 has been reported to methylate and regulate several nonhistone proteins relevant to cancer, including mitogen-activated protein kinase kinase kinase 2 (MAP3K2), vascular endothelial growth factor receptor 1 (VEGFR1), and the human epidermal growth factor receptor 2 (HER2). In addition, overexpression of SMYD3 has been linked to poor prognosis in certain cancers, suggesting SMYD3 as a potential oncogene and

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25

Murphy, James M., Qingwei Zhang, Samuel N. Young, et al. "A robust methodology to subclassify pseudokinases based on their nucleotide-binding properties." Biochemical Journal 457, no. 2 (2013): 323–34. http://dx.doi.org/10.1042/bj20131174.

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We describe the application of a thermal-shift assay to characterize the nucleotide-binding properties of 31 diverse pseudokinase domains. These data support the notion that pseudokinases predominantly serve non-catalytic functions in cellular signalling.

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26

Martinez Molina, Daniel, and Pär Nordlund. "The Cellular Thermal Shift Assay: A Novel Biophysical Assay for In Situ Drug Target Engagement and Mechanistic Biomarker Studies." Annual Review of Pharmacology and Toxicology 56, no. 1 (2016): 141–61. http://dx.doi.org/10.1146/annurev-pharmtox-010715-103715.

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27

Mortison, Jonathan D., Ivan Cornella-Taracido, Gireedhar Venkatchalam, Anthony W. Partridge, Nirodhini Siriwardana, and Simon M. Bushell. "Rapid Evaluation of Small Molecule Cellular Target Engagement with a Luminescent Thermal Shift Assay." ACS Medicinal Chemistry Letters 12, no. 8 (2021): 1288–94. http://dx.doi.org/10.1021/acsmedchemlett.1c00276.

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28

Seashore-Ludlow, Brinton, Hanna Axelsson, Helena Almqvist, Björn Dahlgren, Mats Jonsson, and Thomas Lundbäck. "Quantitative Interpretation of Intracellular Drug Binding and Kinetics Using the Cellular Thermal Shift Assay." Biochemistry 57, no. 48 (2018): 6715–25. http://dx.doi.org/10.1021/acs.biochem.8b01057.

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29

Hashimoto, Mari, Enrico Girardi, Ruth Eichner, and Giulio Superti-Furga. "Detection of Chemical Engagement of Solute Carrier Proteins by a Cellular Thermal Shift Assay." ACS Chemical Biology 13, no. 6 (2018): 1480–86. http://dx.doi.org/10.1021/acschembio.8b00270.

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30

Dziekan, Jerzy M., Han Yu, Dan Chen, et al. "Identifying purine nucleoside phosphorylase as the target of quinine using cellular thermal shift assay." Science Translational Medicine 11, no. 473 (2019): eaau3174. http://dx.doi.org/10.1126/scitranslmed.aau3174.

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Mechanisms of action (MoAs) have been elusive for most antimalarial drugs in clinical use. Decreasing responsiveness to antimalarial treatments stresses the need for a better resolved understanding of their MoAs and associated resistance mechanisms. In the present work, we implemented the cellular thermal shift assay coupled with mass spectrometry (MS-CETSA) for drug target identification inPlasmodium falciparum, the main causative agent of human malaria. We validated the efficacy of this approach for pyrimethamine, a folic acid antagonist, and E64d, a broad-spectrum cysteine proteinase inhibi

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31

Liu, Wen-Wen, Ying Zhu, and Qun Fang. "Femtomole-Scale High-Throughput Screening of Protein Ligands with Droplet-Based Thermal Shift Assay." Analytical Chemistry 89, no. 12 (2017): 6678–85. http://dx.doi.org/10.1021/acs.analchem.7b00899.

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32

Savych, Olena V., Anastasia V. Gryniukova, Diana O. Alieksieieva, et al. "The iterative application of a large chemical space in the drug discovery process." Journal of Organic and Pharmaceutical Chemistry 19, no. 4(76) (2021): 3–11. http://dx.doi.org/10.24959/ophcj.21.244362.

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Aim. To demonstrate the advantages of large-scale virtual libraries generated using chemical protocols previously validated in primary steps of the drug discovery process.Results and discussion. Two validated parallel chemistry protocols reported earlier were used to create the chemical space. It was then sampled based on diversity metric, and the sample was subjected to the virtual screening on BRD4 target. Hits of virtual screening were synthesized and tested in the thermal shift assay.Experimental part. The chemical space was generated using commercially available building blocks and synthe

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33

Peng, Liyuan, Jingwen Jiang, Li Zhou, Edouard C. Nice, and Canhua Huang. "A cellular thermal shift assay for detecting amino acid sites involved in drug target engagement." STAR Protocols 3, no. 2 (2022): 101423. http://dx.doi.org/10.1016/j.xpro.2022.101423.

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34

Chatzikyriakidou, Yurie, Do-Hwan Ahn, Emmanuel Nji, and David Drew. "The GFP thermal shift assay for screening ligand and lipid interactions to solute carrier transporters." Nature Protocols 16, no. 12 (2021): 5357–76. http://dx.doi.org/10.1038/s41596-021-00619-w.

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35

Afanador, Gustavo A., Stephen P. Muench, Martin McPhillie, et al. "Discrimination of Potent Inhibitors ofToxoplasma gondiiEnoyl-Acyl Carrier Protein Reductase by a Thermal Shift Assay." Biochemistry 52, no. 51 (2013): 9155–66. http://dx.doi.org/10.1021/bi400945y.

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36

Krishna, Sankar N., Chi-Hao Luan, Rama K. Mishra, et al. "A Fluorescence-Based Thermal Shift Assay Identifies Inhibitors of Mitogen Activated Protein Kinase Kinase 4." PLoS ONE 8, no. 12 (2013): e81504. http://dx.doi.org/10.1371/journal.pone.0081504.

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37

Ding, Yonghui, Kerri A. Ball, Kristofor J. Webb, et al. "On‐Chip Acousto Thermal Shift Assay for Rapid and Sensitive Assessment of Protein Thermodynamic Stability." Small 16, no. 41 (2020): 2003506. http://dx.doi.org/10.1002/smll.202003506.

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38

Seashore-Ludlow, Brinton, Hanna Axelsson, and Thomas Lundbäck. "Perspective on CETSA Literature: Toward More Quantitative Data Interpretation." SLAS DISCOVERY: Advancing the Science of Drug Discovery 25, no. 2 (2019): 118–26. http://dx.doi.org/10.1177/2472555219884524.

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The cellular thermal shift assay (CETSA) was introduced in 2013 to investigate drug–target engagement inside live cells and tissues. As with all thermal shift assays, the response measured by CETSA is not simply governed by ligand affinity to the investigated target protein, but the thermodynamics and kinetics of ligand binding and protein unfolding also contribute to the observed protein stabilization. This limitation is commonly neglected in current applications of the method to validate the target of small-molecule probes. Instead, there is an eagerness to make direct comparisons of CETSA m

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39

Venkatraman, Janani, Jyothi Bhat, Suresh M. Solapure, et al. "Screening, Identification, and Characterization of Mechanistically Diverse Inhibitors of the Mycobacterium Tuberculosis Enzyme, Pantothenate Kinase (CoaA)." Journal of Biomolecular Screening 17, no. 3 (2011): 293–302. http://dx.doi.org/10.1177/1087057111423069.

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The authors describe the discovery of anti-mycobacterial compounds through identifying mechanistically diverse inhibitors of the essential Mycobacterium tuberculosis ( Mtb) enzyme, pantothenate kinase (CoaA). Target-driven drug discovery technologies often work with purified enzymes, and inhibitors thus discovered may not optimally inhibit the form of the target enzyme predominant in the bacterial cell or may not be available at the desired concentration. Therefore, in addition to addressing entry or efflux issues, inhibitors with diverse mechanisms of inhibition (MoI) could be prioritized bef

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40

Dziekan, Jerzy Michal, Grennady Wirjanata, Lingyun Dai, et al. "Cellular thermal shift assay for the identification of drug–target interactions in the Plasmodium falciparum proteome." Nature Protocols 15, no. 6 (2020): 1881–921. http://dx.doi.org/10.1038/s41596-020-0310-z.

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41

Sviben, Dora, Branimir Bertoša, Andrea Hloušek-Kasun, Dubravko Forcic, Beata Halassy, and Marija Brgles. "Investigation of the thermal shift assay and its power to predict protein and virus stabilizing conditions." Journal of Pharmaceutical and Biomedical Analysis 161 (November 2018): 73–82. http://dx.doi.org/10.1016/j.jpba.2018.08.017.

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42

Giuliani, Sarah E., Ashley M. Frank, and Frank R. Collart. "Functional Assignment of Solute-Binding Proteins of ABC Transporters Using a Fluorescence-Based Thermal Shift Assay†." Biochemistry 47, no. 52 (2008): 13974–84. http://dx.doi.org/10.1021/bi801648r.

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43

Friman, Tomas. "Mass spectrometry-based Cellular Thermal Shift Assay (CETSA®) for target deconvolution in phenotypic drug discovery." Bioorganic & Medicinal Chemistry 28, no. 1 (2020): 115174. http://dx.doi.org/10.1016/j.bmc.2019.115174.

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44

Kalim Bari, Naimat, Gaurav Kumar, Simerpreet Kaur, and Sharmistha Sinha. "Probing and Differentiating the Shell and Enzyme Proteins of the Bacterial Microcompartment by Thermal Shift Assay." Biophysical Journal 116, no. 3 (2019): 62a—63a. http://dx.doi.org/10.1016/j.bpj.2018.11.383.

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45

Senaweera, Sameera, Haijuan Du, Huanchun Zhang, et al. "Discovery of New Small Molecule Hits as Hepatitis B Virus Capsid Assembly Modulators: Structure and Pharmacophore-Based Approaches." Viruses 13, no. 5 (2021): 770. http://dx.doi.org/10.3390/v13050770.

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Hepatitis B virus (HBV) capsid assembly modulators (CpAMs) have shown promise as potent anti-HBV agents in both preclinical and clinical studies. Herein, we report our efforts in identifying novel CpAM hits via a structure-based virtual screening against a small molecule protein-protein interaction (PPI) library, and pharmacophore-guided compound design and synthesis. Curated compounds were first assessed in a thermal shift assay (TSA), and the TSA hits were further evaluated in an antiviral assay. These efforts led to the discovery of two structurally distinct scaffolds, ZW-1841 and ZW-1847,

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46

Wang, Jingjing, Weina Hu, and Qiongbo Hu. "BmTudor-sn Is a Binding Protein of Destruxin A in Silkworm Bm12 Cells." Toxins 11, no. 2 (2019): 67. http://dx.doi.org/10.3390/toxins11020067.

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Destruxin A (DA), a hexa-cyclodepsipeptidic mycotoxin secreted by the entomopathogenic fungus Metarhizium anisopliae, was reported to have an insecticidal effect and anti-immunity activity. However, its molecular mechanism of action remains unclear. Previously, we isolated several potential DA-affinity (binding) proteins in the Bombyx mori Bm12 cell line. By docking score using MOE2015, we selected three proteins—BmTudor-sn, BmPiwi, and BmAGO2—for further validation. First, using Bio-Layer Interferometry in vitro, we found that BmTudor-sn had an affinity interaction with DA at 125, 250, and 50

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47

Al-Amin, Rasel A., Caroline J. Gallant, Phathutshedzo M. Muthelo, and Ulf Landegren. "Sensitive Measurement of Drug-Target Engagement by a Cellular Thermal Shift Assay with Multiplex Proximity Extension Readout." Analytical Chemistry 93, no. 31 (2021): 10999–1009. http://dx.doi.org/10.1021/acs.analchem.1c02225.

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48

Betari, Nibal, Kristoffer Sahlholm, Yuta Ishizuka, Knut Teigen, and Jan Haavik. "Discovery and biological characterization of a novel scaffold for potent inhibitors of peripheral serotonin synthesis." Future Medicinal Chemistry 12, no. 16 (2020): 1461–74. http://dx.doi.org/10.4155/fmc-2020-0127.

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Aim: Tryptophan hydroxylase 1 (TPH1) catalyzes serotonin synthesis in peripheral tissues. Selective TPH1 inhibitors may be useful for treating disorders related to serotonin dysregulation. Results & methodology: Screening using a thermal shift assay for TPH1 binders yielded Compound 1 (2-(4-methylphenyl)-1,2-benzisothiazol-3(2 H)-one), which showed high potency (50% inhibition at 98 ± 30 nM) and selectivity for inhibiting TPH over related aromatic amino acid hydroxylases in enzyme activity assays. Structure–activity relationships studies revealed several analogs of 1 showing comparable pot

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49

Schulze, Jessica, Dieter Moosmayer, Joerg Weiske, et al. "Cell-Based Protein Stabilization Assays for the Detection of Interactions between Small-Molecule Inhibitors and BRD4." Journal of Biomolecular Screening 20, no. 2 (2014): 180–89. http://dx.doi.org/10.1177/1087057114552398.

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Bromodomain protein 4 (BRD4), a member of the bromodomain and extra-terminal (BET) protein family, acts as a central element in transcriptional elongation and plays essential roles in cell proliferation. Inhibition of BRD4 binding to acetylated histone tails via its two bromodomains, BD1 and BD2, with small-molecule inhibitors has been shown to be a valid strategy to prevent cancer growth. We have evaluated and established two novel assays that quantify the interaction of transfected BRD4 BD1 with chemical inhibitors inside cultured cells. Both methods are based on the principle of ligand-indu

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Seashore-Ludlow, Brinton, and Thomas Lundbäck. "Early Perspective." Journal of Biomolecular Screening 21, no. 10 (2016): 1019–33. http://dx.doi.org/10.1177/1087057116659256.

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The cellular thermal shift assay (CETSA) was introduced in 2013 as a means to assess drug binding in complex environments such as cell lysates, live cells, and even tissues. The assay principle relies on the well-proven biophysical concept of ligand-induced thermal stabilization of proteins, which in CETSA applications is measured as a persistent presence of soluble protein at elevated temperatures. Given its recent development, we have just started to learn about the benefits and pitfalls of the method as it is applied to a growing number of protein target classes, the majority of which are i

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