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Last update 08 May 2025

Hesperadin

Last update 08 May 2025

Overview

R&D Status

Clinical Result

Translational Medicine

Overview

Basic Info

Drug Type

Small molecule drug

Synonyms-

Target

Aurora B

Action

inhibitors

Mechanism

Aurora B inhibitors(Serine/threonine-protein kinase Aurora-B inhibitors)

Therapeutic Areas-

Active Indication-

Inactive Indication-

Originator Organization

Forschungsinstitut für Molekulare Pathologie GmbH

Active Organization-

Inactive Organization

Forschungsinstitut für Molekulare Pathologie GmbH

License Organization-

Drug Highest PhasePendingPreclinical

First Approval Date-

Regulation-

Structure/Sequence

Molecular FormulaC29H32N4O3S

InChIKeyGLDSKRNGVVYJAB-DQSJHHFOSA-N

CAS Registry422513-13-1

100 Clinical Results associated with Hesperadin

100 Translational Medicine associated with Hesperadin

100 Patents (Medical) associated with Hesperadin

100

Literatures (Medical) associated with Hesperadin

01 May 2025·Journal of Biological Chemistry

Role of noncanonical histone H2A variant, H2A.Z, to maintain proper centromeric transcription and chromosome segregation

Article

Author: Phonesavanh, Tyson ; Lu, Jiaxing ; Akter, Mahmuda ; Wang, Xiao ; Kang, Jungseog ; Yu, Hongtao ; Lyu, Xiaoai ; Wang, Hao

The genome stability of eukaryotic cells is ensured by proper regulation of histones and their variants. H2A.Z, a conserved and essential histone H2A variant, plays a crucial role in this process by regulating various chromatin-related processes such as gene expression, heterochromatin formation, DNA damage repair, and chromosome segregation. It has two isoforms, H2A.Z1 and H2A.Z2, also known as H2AFZ and H2AFV, respectively, which perform both redundant and nonredundant roles in maintaining genome stability. In this study, we investigated the isoform-specific mitotic functions of H2A.Z in HeLa cells. Our studies revealed that the depletion of H2AFV or H2AFZ did not alter the overall cell cycle profile. However, H2AFV depletion significantly increased the formation of micronuclei, indicating defects in chromosome segregation. Additionally, H2AFV depletion led to the accumulation of DNA damage at various nuclear loci including centromeres. Interestingly, we discovered that H2AFV depletion significantly increased centromeric transcription, which may interfere with proper centromere function. Furthermore, we discovered that a mitotic kinase, Aurora B, binds to both H2AFV and H2AFZ, but preferentially to H2AFV. Inhibition of Aurora B activity by hesperadin disrupted proper centromeric transcription but not significantly centromeric localization of H2A.Z. Collectively, these data demonstrated that the H2A.Z isoforms play distinctive regulatory roles in maintaining proper centromeric transcription and DNA repair, ensuring accurate chromosome segregation.

01 Mar 2025·Advanced Science

Ischemic Area‐Targeting and Self‐Monitoring Nanoprobes Ameliorate Myocardial Ischemia/Reperfusion Injury by Scavenging ROS and Counteracting Cardiac Inflammation

Article

Author: Nie, Liming ; Fan, Zhijin ; Ma, Xiaobin ; Peng, Jingyan

AbstractPrecise and effective management of myocardial ischemia/reperfusion injury (MIRI) is still a formidable challenge in clinical practice. Additionally, real‐time monitoring of drug aggregation in the MIRI region remains an open question. Herein, a drug delivery system, hesperadin and ICG assembled in PLGA‐Se‐Se‐PEG‐IMTP (HI@PSeP‐IMTP), is designed to deliver hesperadin and ICG to the MIRI region for in vivo optical imaging tracking and to ameliorate MIRI. The peak aggregation of nanoprobes in the MIRI region is monitored by near‐infrared fluorescence and photoacoustic imaging. The maximal fluorescence and photoacoustic signals of the HI@PSeP‐IMTP group in the MIRI region rise ≈32% and 40% respectively compared with that of HI@PSeP group. Moreover, HI@PSeP‐IMTP effectively mitigates MIRI due to a synergistic integration of diselenide bonds and hesperadin, which can eliminate ROS and suppress cardiac inflammation. Specifically, the expression levels of p‐CaMKII, p‐IκBα, and p65 in the MIRI region in the HI@PSeP‐IMTP group demonstrate a reduction of 30%, 46%, and 42% respectively compared to that of the PBS group. Collectively, HI@PSeP‐IMTP provides new insights into the development of drugs integrating diagnosis and treatment for MIRI.

01 Mar 2025·International Journal of Biological Macromolecules

Identification of chemical inhibitors targeting long noncoding RNA through gene signature-based high throughput screening

Article

Author: Gui, Yu ; Wang, Yumei ; Li, Shengrong ; Lin, Kequan ; Yu, Xiankuo ; An, Jun ; Huang, Lijun ; Wei, Mingming ; Liao, Yile ; Wang, Dong ; Tan, Xue ; Wang, Huili ; Hu, Chao ; Luo, Yan

Scalable methods for functionally high-throughput screening of RNA-targeting small molecules are currently limited. Here, an RNA knockdown gene signature and high-throughput sequencing-based high-throughput screening (HTS²) were integrated to identify RNA-targeting compounds. We first generated a gene signature characterizing the knockdown of the long non-coding RNA LINC00973. Then, screening of 8199 compounds by HTS² assay identified that treatments of Hesperadin and GSK1070916 significantly mimic the expression pattern of the LINC00973 knockdown gene signature. Functionally, cell phenotype changes after treatments of these two compounds also mimic the losing function of LINC00973 in multiple types of cancer cells. Mechanistically, the inhibitory action of these two compounds on LINC00973 primarily operates via the AURKB-mediated MAPK signaling pathway, resulting in reduced expression of the transcription factor c-Jun. Consequently, this leads to the suppression of LINC00973 transcription. Moreover, these two compounds significantly inhibit xenograft tumor growth in vivo. Clinically, we further found that breast tumors with high expression of LINC00973 also show relatively high expression of AURKB or JUN, and vice versa. In summary, we established a novel high-throughput screening strategy to identify small molecules capable of targeting RNA, provided two promising compounds targeting LINC00973 and further shed light on the underlying transcriptional upregulation mechanism of LINC00973 within cancer cells.

100 Deals associated with Hesperadin

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Hesperadin

Overview

Basic Info

Structure/Sequence

Related

R&D Status

Clinical Result

Translational Medicine

Deal

Core Patent

Clinical Trial

Approval

Regulation