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作为p53-Y220C裂结合剂,具有多种结合方式的SNAr反应性皮拉津衍生物

Theresa Klett1, Jason Stahlecker1, Martin Schwer1

  • 1Laboratory for Molecular Design & Pharmaceutical Biophysics, Institute of Pharmaceutical Sciences, Department of Pharmacy and Biochemistry, Eberhard Karls Universität Tübingen, Tübingen, 72076, Germany.

Drug design, development and therapy
|July 2, 2025
PubMed
概括

研究人员开发了新的pyrazine衍生物来稳定常见的与癌症相关的p53-Y220C突变. 化合物SN006/7-8显著增强了热稳定性,为p53突变癌症提供了一个有前途的治疗途径.

关键词:
在X射线晶体学.基于共价片段的药物发现.不同扫描光仪的差异扫描光仪.完整的蛋白质质量谱仪质量谱仪.结构-活动关系关系.瘤抑制剂 p53 突变稳定剂

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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