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一种用于测量配体与生物组织中未知浓度蛋白质结合亲和力的直接方法。

A straightforward method for measuring binding affinities of ligands to proteins of unknown concentration in biological tissues.

作者信息

Yan Bin, Bunch Josephine

机构信息

National Centre of Excellence in Mass Spectrometry Imaging, National Physical Laboratory Hampton Road Teddington TW11 0LW UK

Department of Metabolism, Digestion and Reproduction, Imperial College London, Hammersmith Hospital Du Cane Road London W12 0NN UK

出版信息

Chem Sci. 2025 Apr 11;16(20):8673-8681. doi: 10.1039/d5sc02460a. eCollection 2025 May 21.

DOI:10.1039/d5sc02460a
PMID:40313517
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12042207/
Abstract

The equilibrium dissociation constant ( ) is a quantitative measure of the strength with which a drug binds to its receptor. Methods for determining typically require knowledge of protein concentration or mass. We report a simple dilution method for estimation of using native mass spectrometry which can be applied to protein-ligand complexes involving proteins of unknown concentration, from complex mixtures, including direct tissue sampling.

摘要

平衡解离常数（ ）是衡量药物与其受体结合强度的定量指标。测定 的方法通常需要知道蛋白质的浓度或质量。我们报告了一种使用原生质谱法估算 的简单稀释方法，该方法可应用于涉及未知浓度蛋白质的蛋白质-配体复合物，这些复合物来自复杂混合物，包括直接组织采样。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b90a/12093516/4e4eff92a121/d5sc02460a-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b90a/12093516/f6c7758f6150/d5sc02460a-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b90a/12093516/4e4eff92a121/d5sc02460a-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b90a/12093516/f6c7758f6150/d5sc02460a-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b90a/12093516/4e4eff92a121/d5sc02460a-f2.jpg

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Deciphering Pathways and Thermodynamics of Protein Assembly Using Native Mass Spectrometry.利用天然质谱法破译蛋白质组装的途径和热力学。
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Laser capture microdissection and native mass spectrometry for spatially-resolved analysis of intact protein assemblies in tissue.
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