Univ. Lille, CNRS, Inserm, CHU Lille, UMR9020-UMR1277-Canther-Cancer Heterogeneity, Plasticity and Resistance to Therapies, 59000 Lille, France.
Oncowitan, Scientific Consulting Office, 59045 Lille, France.
Int J Mol Sci. 2022 Jul 12;23(14):7672. doi: 10.3390/ijms23147672.
The review highlights how protein-protein interactions (PPIs) have determining roles in most life processes and how interactions between protein partners are involved in various human diseases. The study of PPIs and binding interactions as well as their understanding, quantification and pharmacological regulation are crucial for therapeutic purposes. Diverse computational and analytical methods, combined with high-throughput screening (HTS), have been extensively used to characterize multiple types of PPIs, but these procedures are generally laborious, long and expensive. Rapid, robust and efficient alternative methods are proposed, including the use of Microscale Thermophoresis (MST), which has emerged as the technology of choice in drug discovery programs in recent years. This review summarizes selected case studies pertaining to the use of MST to detect therapeutically pertinent proteins and highlights the biological importance of binding interactions, implicated in various human diseases. The benefits and limitations of MST to study PPIs and to identify regulators are discussed.
该综述强调了蛋白质-蛋白质相互作用 (PPIs) 在大多数生命过程中所起的决定性作用,以及蛋白质伴侣之间的相互作用如何涉及各种人类疾病。PPIs 和结合相互作用的研究及其理解、量化和药理学调节对于治疗目的至关重要。各种计算和分析方法,结合高通量筛选 (HTS),已被广泛用于表征多种类型的 PPI,但这些程序通常费力、耗时且昂贵。因此提出了快速、稳健和高效的替代方法,包括使用微量热泳动 (MST),近年来该技术已成为药物发现项目中首选的技术。本文综述了使用 MST 检测治疗相关蛋白的选定案例研究,并强调了与各种人类疾病相关的结合相互作用的生物学重要性。讨论了 MST 研究 PPI 和鉴定调节剂的优势和局限性。