Advancing the development of TRIP13 inhibitors: A high-throughput screening approach

TRIP13, a promising target for cancer therapy, has been identified as a key regulator of the mitotic checkpoint. Overexpression of TRIP13 is associated with poor clinical outcomes in various cancers. Inhibition of TRIP13 has the potential to address therapeutic challenges in cancer, particularly in...

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Main Authors: Rae M. Sammons, Soma Ghosh, Lacin Yapindi, Eun Jeong Cho, Faye M. Johnson, Kevin N. Dalby
Format: Article
Language:English
Published: Elsevier 2025-06-01
Series:SLAS Discovery
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Online Access:http://www.sciencedirect.com/science/article/pii/S2472555225000267
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author Rae M. Sammons
Soma Ghosh
Lacin Yapindi
Eun Jeong Cho
Faye M. Johnson
Kevin N. Dalby
author_facet Rae M. Sammons
Soma Ghosh
Lacin Yapindi
Eun Jeong Cho
Faye M. Johnson
Kevin N. Dalby
author_sort Rae M. Sammons
collection DOAJ
description TRIP13, a promising target for cancer therapy, has been identified as a key regulator of the mitotic checkpoint. Overexpression of TRIP13 is associated with poor clinical outcomes in various cancers. Inhibition of TRIP13 has the potential to address therapeutic challenges in cancer, particularly in therapy-resistant and Rb-deficient cancers. Despite the potential therapeutic benefits of TRIP13 inhibition, the development of TRIP13 inhibitors has been hindered by the lack of a robust high-throughput screening (HTS) assay.We developed a luminescence-based biochemical assay for TRIP13 activity to address this challenge using the ADP-Glo detection system. This assay offers high sensitivity, low background signal, and ease of automation, making it ideal for HTS applications. A pilot screen of kinase-focused inhibitors library and a large-scale screen of 4000 additional compounds demonstrated the assay's robust performance with a z'-factor exceeding 0.85 and a signal-to-background (S/B) ratio near 6. From the 50 initial hits, rigorous validation identified anlotinib as the most potent TRIP13 inhibitor with an IC50 of 5 μM. A cellular thermal shift assay (CETSA) confirmed the direct binding of anlotinib to TRIP13, validating the potential of our biochemical assay for identifying novel TRIP13 inhibitors. Our study provides a valuable tool for discovering novel TRIP13 inhibitors and advances our understanding of the therapeutic potential of targeting TRIP13 in cancer.
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spelling doaj-art-bef6f7e7ff2849f8855b1df4ed875e532025-08-20T01:49:08ZengElsevierSLAS Discovery2472-55522025-06-013310023310.1016/j.slasd.2025.100233Advancing the development of TRIP13 inhibitors: A high-throughput screening approachRae M. Sammons0Soma Ghosh1Lacin Yapindi2Eun Jeong Cho3Faye M. Johnson4Kevin N. Dalby5Targeted Therapeutic Drug Discovery & Development Program, The University of Texas at Austin, Austin, TX, United StatesThoracic, Head and Neck Medical Oncology, The University of Texas, MD Anderson Cancer Center, Houston, TX, United StatesThoracic, Head and Neck Medical Oncology, The University of Texas, MD Anderson Cancer Center, Houston, TX, United StatesTargeted Therapeutic Drug Discovery & Development Program, The University of Texas at Austin, Austin, TX, United States; Corresponding authors.Thoracic, Head and Neck Medical Oncology, The University of Texas, MD Anderson Cancer Center, Houston, TX, United StatesTargeted Therapeutic Drug Discovery & Development Program, The University of Texas at Austin, Austin, TX, United States; Division of Chemical Biology & Medicinal Chemistry, College of Pharmacy, The University of Texas at Austin, Austin, TX, United States; Corresponding authors.TRIP13, a promising target for cancer therapy, has been identified as a key regulator of the mitotic checkpoint. Overexpression of TRIP13 is associated with poor clinical outcomes in various cancers. Inhibition of TRIP13 has the potential to address therapeutic challenges in cancer, particularly in therapy-resistant and Rb-deficient cancers. Despite the potential therapeutic benefits of TRIP13 inhibition, the development of TRIP13 inhibitors has been hindered by the lack of a robust high-throughput screening (HTS) assay.We developed a luminescence-based biochemical assay for TRIP13 activity to address this challenge using the ADP-Glo detection system. This assay offers high sensitivity, low background signal, and ease of automation, making it ideal for HTS applications. A pilot screen of kinase-focused inhibitors library and a large-scale screen of 4000 additional compounds demonstrated the assay's robust performance with a z'-factor exceeding 0.85 and a signal-to-background (S/B) ratio near 6. From the 50 initial hits, rigorous validation identified anlotinib as the most potent TRIP13 inhibitor with an IC50 of 5 μM. A cellular thermal shift assay (CETSA) confirmed the direct binding of anlotinib to TRIP13, validating the potential of our biochemical assay for identifying novel TRIP13 inhibitors. Our study provides a valuable tool for discovering novel TRIP13 inhibitors and advances our understanding of the therapeutic potential of targeting TRIP13 in cancer.http://www.sciencedirect.com/science/article/pii/S2472555225000267TRIP13ATPaseRb-deficient cancersLuminescenceHigh throughput compound screening
spellingShingle Rae M. Sammons
Soma Ghosh
Lacin Yapindi
Eun Jeong Cho
Faye M. Johnson
Kevin N. Dalby
Advancing the development of TRIP13 inhibitors: A high-throughput screening approach
SLAS Discovery
TRIP13
ATPase
Rb-deficient cancers
Luminescence
High throughput compound screening
title Advancing the development of TRIP13 inhibitors: A high-throughput screening approach
title_full Advancing the development of TRIP13 inhibitors: A high-throughput screening approach
title_fullStr Advancing the development of TRIP13 inhibitors: A high-throughput screening approach
title_full_unstemmed Advancing the development of TRIP13 inhibitors: A high-throughput screening approach
title_short Advancing the development of TRIP13 inhibitors: A high-throughput screening approach
title_sort advancing the development of trip13 inhibitors a high throughput screening approach
topic TRIP13
ATPase
Rb-deficient cancers
Luminescence
High throughput compound screening
url http://www.sciencedirect.com/science/article/pii/S2472555225000267
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