磷酸化诱导嵌合小分子的开发-猫眼课题宝

磷酸化诱导嵌合小分子的开发

批准号：

10043054

负责人：

Amit Choudhary

金额：

$24.0万

依托单位：

BROAD INSTITUTE, INC.

依托单位国家：

美国

项目类别：

财政年份：

2020

资助国家：

美国

项目状态：

已结题

起止时间：

2020-08-19 至 2022-07-31

来源：

https://reporter.nih.gov/project-details/10043054

关键词：

5&apos -AMP-activated protein kinase Adaptor Signaling Protein Affinity Agammaglobulinaemia tyrosine kinase Attenuated Binding Biochemical Biological Breathing Bromodomain Cells Chemicals Complex Computer Models Dependence Development Dimerization Dose Enzymes Equilibrium Evaluation Event Exhibits Exploratory/Developmental Grant Future HLA Antigens Immune response Immune system Length Ligands Mediating Membrane Methods Nature Nuclear Pharmaceutical Preparations Phosphorylation Phosphorylation Site Phosphotransferases Play Protac Protein Isoforms Protein Kinase Protein Kinase C Protein Tyrosine Kinase Protein-Serine-Threonine Kinases Proteins Proteomics Research Role Serine/Threonine Phosphorylation Signal Transduction Specificity Structure Tacrolimus Binding Protein 1A Therapeutic Tyrosine Phosphorylation computer studies experimental study immunoregulation interest loss of function multidisciplinary neoantigens phosphoproteomics programs protein function small molecule

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中文摘要

翻译

项目摘要蛋白质磷酸化可以激活、抑制或改变蛋白质的功能。阻止蛋白质的小分子存在通过激酶抑制的磷酸化，但是根据需要诱导任何蛋白质磷酸化的方法并不存在我们建议开发一类新的小分子，称为磷酸化诱导嵌合体小分子（PHICS），通过剂量和时间控制诱导蛋白磷酸化。PHICS 将通过将小分子激酶结合剂与靶蛋白的小分子结合剂连接而形成，使活性激酶接近靶蛋白以启动磷酸化。 1

英文摘要

PROJECT SUMMARY Protein phosphorylation can activate, inhibit, or modify protein’s function. Small molecules that block protein phosphorylation via kinase inhibition exist, but methods to induce phosphorylation of any protein on demand do not exist. We propose to develop a new class of small molecules, termed PHosphorylation Inducing Chimeric Small molecules (PHICS), which will induce protein phosphorylation with dose and temporal control. PHICS will be formed by joining a small-molecule kinase binder with a small-molecule binder of the target protein so that an active kinase is brought into proximity to the target protein to initiate phosphorylation. 1

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