ArticleACS medicinal chemistry letters2015
Structure-Guided Design of Novel l-Cysteine Derivatives as Potent KSP Inhibitors.
Article in ACS medicinal chemistry letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Pharmacophore-Based Structure Optimization ofACS medicinal chemistry letters · 2025Article
- Modular multi-enzyme cascades enable green and sustainable synthesis of non-canonical amino acids from glycerol.Nature communications · 2025Article
- Design of MMP-1 inhibitors via SAR transfer and experimental validation.Scientific reports · 2022Article
- Insights into the Molecular Mechanisms of Eg5 Inhibition by (+)-Morelloflavone.Pharmaceuticals (Basel, Switzerland) · 2019Article
- Structural and Thermodynamic Basis of the Enhanced Interaction between Kinesin Spindle Protein Eg5 and STLC-type Inhibitors.ACS omega · 2018Article
- Recent findings and future directions for interpolar mitotic kinesin inhibitors in cancer therapy.Future medicinal chemistry · 2016Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kinesin spindle protein (KSP), known as Hs Eg5, a member of the kinesin-5 family, plays an important role in the formation and maintenance of the bipolar spindle. We previously reported S-trityl-l-cysteine derivatives as selective KSP inhibitors. Here, we report further optimizations using docking modeling in the L5 allosteric binding site, which led to the discovery of several high affinity derivatives with two fused phenyl rings in the trityl group giving low nanomolar range KSP ATPase inhibition. The representative derivatives potently inhibited cell growth of HCT116 cells in correlation with KSP inhibitory activities and significantly suppressed tumor growth in the xenograft model in vivo.
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