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利用光镊进行力测量来探究活细胞中的配体-受体相互作用

Probing Ligand-Receptor Interaction in Living Cells Using Force Measurements With Optical Tweezers.

作者信息

Riesenberg Carolin, Iriarte-Valdez Christian Alejandro, Becker Annegret, Dienerowitz Maria, Heisterkamp Alexander, Ngezahayo Anaclet, Torres-Mapa Maria Leilani

机构信息

Institute of Quantum Optics, Leibniz University Hannover, Hannover, Germany.

Lower Saxony Centre for Biomedical Engineering, Implant Research and Development (NIFE), Hannover, Germany.

出版信息

Front Bioeng Biotechnol. 2020 Nov 17;8:598459. doi: 10.3389/fbioe.2020.598459. eCollection 2020.

DOI:10.3389/fbioe.2020.598459
PMID:33282853
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7705203/
Abstract

This work probes the binding kinetics of COOH-terminus of (c-CPE) and claudin expressing MCF-7 cells using force spectroscopy with optical tweezers. c-CPE is of high biomedical interest due to its ability to specifically bind to claudin with high affinity as well as reversibly disrupt tight junctions whilst maintaining cell viability. We observed single-step rupture events between silica particles functionalized with c-CPE and MCF-7 cells. Extensive calibration of the optical tweezers' trap stiffness and displacement of the particle from trap center extracted a probable bond rupture force of ≈ 18 pN. The probability of rupture events with c-CPE functionalized silica particles increased by 50% compared to unfunctionalized particles. Additionally, rupture events were not observed when probing cells not expressing claudin with c-CPE coated particles. Overall, this work demonstrates that optical tweezers are invaluable tools to probe ligand-receptor interactions and their potential to study dynamic molecular events in drug-binding scenarios.

摘要

这项工作使用光镊力谱法探究了（c-CPE）羧基末端与表达claudin的MCF-7细胞之间的结合动力学。c-CPE具有很高的生物医学研究价值，因为它能够以高亲和力特异性结合claudin，并能在维持细胞活力的同时可逆地破坏紧密连接。我们观察到用c-CPE功能化的二氧化硅颗粒与MCF-7细胞之间的单步破裂事件。通过对光镊阱刚度的广泛校准以及颗粒从阱中心的位移，得出可能的键断裂力约为18 pN。与未功能化的颗粒相比，用c-CPE功能化的二氧化硅颗粒发生破裂事件的概率增加了50%。此外，当用c-CPE包被的颗粒探测不表达claudin的细胞时，未观察到破裂事件。总的来说，这项工作表明光镊是探测配体-受体相互作用及其在药物结合场景中研究动态分子事件潜力的宝贵工具。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/6f065d51d3b5/fbioe-08-598459-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/4730ed930501/fbioe-08-598459-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/6c37a5a24805/fbioe-08-598459-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/1bdd6d4dd3c2/fbioe-08-598459-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/499ab5100d9d/fbioe-08-598459-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/d922f2c406ea/fbioe-08-598459-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/c6db99eb9d8a/fbioe-08-598459-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/6f065d51d3b5/fbioe-08-598459-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/4730ed930501/fbioe-08-598459-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/6c37a5a24805/fbioe-08-598459-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/1bdd6d4dd3c2/fbioe-08-598459-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/499ab5100d9d/fbioe-08-598459-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/d922f2c406ea/fbioe-08-598459-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/c6db99eb9d8a/fbioe-08-598459-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8d06/7705203/6f065d51d3b5/fbioe-08-598459-g007.jpg

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