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设计“狙击手”:通过分子模拟改进用于抗癌治疗的靶向人细胞溶解融合蛋白

Designing the Sniper: Improving Targeted Human Cytolytic Fusion Proteins for Anti-Cancer Therapy via Molecular Simulation.

作者信息

Bochicchio Anna, Jordaan Sandra, Losasso Valeria, Chetty Shivan, Perera Rodrigo Casasnovas, Ippoliti Emiliano, Barth Stefan, Carloni Paolo

机构信息

German Research School for Simulation Sciences, Forschungszentrum Jülich, Jülich 52425, Germany.

Computational Biomedicine, Institute for Advanced Simulation IAS-5 and Institute of Neuroscience and Medicine INM-9, Forschungszentrum Jülich, Jülich 52425, Germany.

出版信息

Biomedicines. 2017 Feb 17;5(1):9. doi: 10.3390/biomedicines5010009.

Abstract

Targeted human cytolytic fusion proteins (hCFPs) are humanized immunotoxins for selective treatment of different diseases including cancer. They are composed of a ligand specifically binding to target cells genetically linked to a human apoptosis-inducing enzyme. hCFPs target cancer cells via an antibody or derivative (scFv) specifically binding to e.g., tumor associated antigens (TAAs). After internalization and translocation of the enzyme from endocytosed endosomes, the human enzymes introduced into the cytosol are efficiently inducing apoptosis. Under in vivo conditions such enzymes are subject to tight regulation by native inhibitors in order to prevent inappropriate induction of cell death in healthy cells. Tumor cells are known to upregulate these inhibitors as a survival mechanism resulting in escape of malignant cells from elimination by immune effector cells. Cytosolic inhibitors of Granzyme B and Angiogenin (Serpin P9 and RNH1, respectively), reduce the efficacy of hCFPs with these enzymes as effector domains, requiring detrimentally high doses in order to saturate inhibitor binding and rescue cytolytic activity. Variants of Granzyme B and Angiogenin might feature reduced affinity for their respective inhibitors, while retaining or even enhancing their catalytic activity. A powerful tool to design hCFPs mutants with improved potency is given by in silico methods. These include molecular dynamics (MD) simulations and enhanced sampling methods (ESM). MD and ESM allow predicting the enzyme-protein inhibitor binding stability and the associated conformational changes, provided that structural information is available. Such "high-resolution" detailed description enables the elucidation of interaction domains and the identification of sites where particular point mutations may modify those interactions. This review discusses recent advances in the use of MD and ESM for hCFP development from the viewpoints of scientists involved in both fields.

摘要

靶向人细胞溶解融合蛋白(hCFP)是用于选择性治疗包括癌症在内的不同疾病的人源化免疫毒素。它们由与人类凋亡诱导酶基因相连的特异性结合靶细胞的配体组成。hCFP通过特异性结合例如肿瘤相关抗原(TAA)的抗体或衍生物(单链抗体片段)靶向癌细胞。在酶从内吞的内体内化和转运后,引入细胞质中的人类酶可有效诱导细胞凋亡。在体内条件下,此类酶受到天然抑制剂的严格调控,以防止在健康细胞中不适当诱导细胞死亡。已知肿瘤细胞会上调这些抑制剂作为一种生存机制,导致恶性细胞逃避免疫效应细胞的清除。颗粒酶B和血管生成素的细胞质抑制剂(分别为丝氨酸蛋白酶抑制剂P9和核糖核酸酶抑制因子1)降低了以这些酶作为效应域的hCFP的功效,需要使用有害的高剂量才能饱和抑制剂结合并挽救细胞溶解活性。颗粒酶B和血管生成素的变体可能对其各自的抑制剂具有降低的亲和力,同时保留甚至增强其催化活性。计算机方法为设计具有更高效力的hCFP突变体提供了一个强大的工具。这些方法包括分子动力学(MD)模拟和增强采样方法(ESM)。如果有结构信息,MD和ESM可以预测酶-蛋白质抑制剂的结合稳定性以及相关的构象变化。这种“高分辨率”的详细描述能够阐明相互作用域,并识别特定点突变可能改变这些相互作用的位点。本综述从这两个领域的科学家的角度讨论了MD和ESM在hCFP开发中的最新进展。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f180/5423494/f8e614f19c07/biomedicines-05-00009-g001.jpg

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