基于荧光偏振的组织蛋白酶L抑制剂高通量筛选试验。

IF 1.1 Q3 BIOLOGY
Keyu Guo, Baoqing You, Wenwen Zhou, Yan Li, Zhen Wang, Jing Zhang, Shuyi Si
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引用次数: 0

摘要

组织蛋白酶L (CTSL)是一种溶酶体半胱氨酸蛋白酶,属于木瓜蛋白酶家族,主要参与细胞内蛋白质降解、抗原加工和细胞外基质重塑。由于活性失调或过度表达,它在病理条件中起着关键作用,包括癌症转移、神经退行性疾病和病毒感染。因此,针对CTSL的抑制剂正在研究治疗应用。目前鉴定CTSL抑制剂的方法主要依赖于荧光标记的底物、荧光共振能量转移(FRET)和基于细胞的筛选试验。在这里,我们将荧光偏振(FP)原理应用于CTSL通过毫极化单位(mp)值的变化检测底物裂解活性,并建立了一种成本效益高、定量、节省试剂和时间的抑制剂高通量筛选(HTS)方法。我们还提供了从真核细胞中表达和纯化高活性CTSL的详细步骤,为基于fp的检测奠定了坚实的基础。该分析的一个关键优势在于其对荧光干扰的敏感性降低,因为异硫氰酸荧光素(FITC)荧光团在535 nm处具有高量子效率,其发射峰与大多数天然荧光分子的波长范围不同。该检测对反应时间、温度和二甲基亚砜(DMSO)浓度的适应性最大限度地减少了由轻微实验不一致引起的假阳性或假阴性结果,简化了筛选过程。此外,与传统方法相比,该方案需要更少的操作步骤、更短的孵育时间和更少的CTSL和底物数量。这种快速、经济、可扩展的方法非常符合HTS平台的需求。•活性重组CTSL的真核表达、纯化和鉴定及其生物活性测定的详细程序。•针对CTSL的基于荧光偏振(FP)的高通量筛选(HTS)检测应用的完整描述。•阐述基于fp的分析在CTSL活性评估或药物发现中的应用。•协议很容易适用于具有类似催化机制的其他蛋白酶。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Fluorescence Polarization-Based High-Throughput Screening Assay for Inhibitors Targeting Cathepsin L.

Fluorescence Polarization-Based High-Throughput Screening Assay for Inhibitors Targeting Cathepsin L.

Fluorescence Polarization-Based High-Throughput Screening Assay for Inhibitors Targeting Cathepsin L.

Fluorescence Polarization-Based High-Throughput Screening Assay for Inhibitors Targeting Cathepsin L.

Cathepsin L (CTSL), a lysosomal cysteine protease belonging to the papain-like protease family, is primarily involved in intracellular protein degradation, antigen processing, and extracellular matrix remodeling. It plays critical roles in pathological conditions, including cancer metastasis, neurodegenerative disorders, and viral infection, due to dysregulated activity or overexpression. Thus, inhibitors targeting CTSL are under investigation for therapeutic applications. Current approaches for identifying CTSL inhibitors predominantly rely on fluorescence-labeled substrates, fluorescence resonance energy transfer (FRET), and cell-based screening assays. Here, we applied the principle of fluorescence polarization (FP) to the detection of substrate cleavage activity by CTSL through changes in millipolarization unit (mp) values and established a cost-effective, quantitative, reagent- and time-saving inhibitor high-throughput screening (HTS) assay. We also provide detailed steps for the expression and purification of highly active CTSL from eukaryotic cells, which lays a solid foundation for the FP-based assay. A key advantage of this assay lies in its reduced susceptibility to fluorescence interference, as the fluorescein isothiocyanate (FITC) fluorophore exhibits high quantum efficiency with an emission peak at 535 nm-a wavelength range distinct from most naturally occurring fluorescent molecules. The assay's adaptability to reaction time, temperature, and dimethyl sulfoxide (DMSO) concentration minimizes false-positive or false-negative results caused by minor experimental inconsistencies, streamlining the screening process. Furthermore, the protocol requires fewer operational steps, reduced incubation time, and lower quantities of CTSL and substrates compared to conventional methods. This rapid, cost-effective, and scalable approach aligns well with the demands of HTS platforms. Key features • Detailed procedures for eukaryotic expression, purification, and identification of active recombinant CTSL and determination of its biological activity. • Full description for application of fluorescence polarization (FP)-based high-throughput screening (HTS) assay targeting CTSL. • Elaboration for the application of the FP-based assay in CTSL activity evaluation or drug discovery. • Protocol is readily adaptable to other proteases with a similar catalytic mechanism.

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