Manning College of Information and Computer Science, University of Massachusetts, Amherst, MA 01003, USA.
Applied Physics, 477 Madison Ave., 6th Floor, New York, NY 10022, USA.
Int J Mol Sci. 2023 Sep 27;24(19):14648. doi: 10.3390/ijms241914648.
One of the most important aspects of successful cancer therapy is the identification of a target protein for inhibition interaction. Conventionally, this consists of screening a panel of genes to assess which is mutated and then developing a small molecule to inhibit the interaction of two proteins or to simply inhibit a specific protein from all interactions. In previous work, we have proposed computational methods that analyze protein-protein networks using both topological approaches and thermodynamic quantification provided by Gibbs free energy. In order to make these approaches both easier to implement and free of arbitrary topological filtration criteria, in the present paper, we propose a modification of the topological-thermodynamic analysis, which focuses on the selection of the most thermodynamically stable proteins and their subnetwork interaction partners with the highest expression levels. We illustrate the implementation of the new approach with two specific cases, glioblastoma (glioma brain tumors) and chronic lymphatic leukoma (CLL), based on the publicly available patient-derived datasets. We also discuss how this can be used in clinical practice in connection with the availability of approved and investigational drugs.
癌症治疗成功的一个最重要的方面是确定抑制相互作用的靶蛋白。传统上,这包括筛选一组基因以评估哪些基因发生了突变,然后开发一种小分子来抑制两种蛋白质的相互作用,或者简单地抑制特定蛋白质的所有相互作用。在之前的工作中,我们提出了使用拓扑方法和由吉布斯自由能提供的热力学定量分析蛋白质-蛋白质网络的计算方法。为了使这些方法更易于实现并且不受任意拓扑过滤标准的限制,在本文中,我们提出了对拓扑-热力学分析的修改,该方法侧重于选择热力学最稳定的蛋白质及其具有最高表达水平的子网络相互作用伙伴。我们使用两个具体案例(神经胶质瘤(脑肿瘤)和慢性淋巴细胞白血病(CLL)),基于公开的患者衍生数据集来说明新方法的实现。我们还讨论了如何在与现有批准药物和研究性药物的可用性相关的临床实践中使用这种方法。