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磁悬浮技术作为一种竞争性蛋白质配体结合分析的平台。

Magnetic levitation as a platform for competitive protein-ligand binding assays.

机构信息

Department of Chemistry & Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United States.

出版信息

Anal Chem. 2012 Jul 17;84(14):6166-72. doi: 10.1021/ac301121z. Epub 2012 Jun 28.

Abstract

This paper describes a method based on magnetic levitation (MagLev) that is capable of indirectly measuring the binding of unlabeled ligands to unlabeled protein. We demonstrate this method by measuring the affinity of unlabeled bovine carbonic anhydrase (BCA) for a variety of ligands (most of which are benzene sulfonamide derivatives). This method utilizes porous gel beads that are functionalized with a common aryl sulfonamide ligand. The beads are incubated with BCA and allowed to reach an equilibrium state in which the majority of the immobilized ligands are bound to BCA. Since the beads are less dense than the protein, protein binding to the bead increases the overall density of the bead. This change in density can be monitored using MagLev. Transferring the beads to a solution containing no protein creates a situation where net protein efflux from the bead is thermodynamically favorable. The rate at which protein leaves the bead for the solution can be calculated from the rate at which the levitation height of the bead changes. If another small molecule ligand of BCA is dissolved in the solution, the rate of protein efflux is accelerated significantly. This paper develops a reaction-diffusion (RD) model to explain both this observation, and the physical-organic chemistry that underlies it. Using this model, we calculate the dissociation constants of several unlabeled ligands from BCA, using plots of levitation height versus time. Notably, although this method requires no electricity, and only a single piece of inexpensive equipment, it can measure accurately the binding of unlabeled proteins to small molecules over a wide range of dissociation constants (K(d) values within the range from ~10 nM to 100 μM are measured easily). Assays performed using this method generally can be completed within a relatively short time period (20 min-2 h). A deficiency of this system is that it is not, in its present form, applicable to proteins with molecular weight greater than approximately 65 kDa.

摘要

本文描述了一种基于磁悬浮(MagLev)的方法,该方法能够间接测量未标记配体与未标记蛋白的结合。我们通过测量未标记的牛碳酸酐酶(BCA)与各种配体(其中大多数为苯磺酰胺衍生物)的亲和力来证明该方法。该方法利用多孔凝胶珠,其用常见的芳基磺酰胺配体官能化。将珠与 BCA 一起孵育,并使其达到平衡状态,其中大多数固定配体与 BCA 结合。由于珠子的密度小于蛋白质,因此蛋白质与珠子结合会增加珠子的整体密度。这种密度变化可以使用 MagLev 进行监测。将珠子转移到不含蛋白质的溶液中会产生从珠子中净蛋白流出的情况,从热力学上看这是有利的。可以从珠的悬浮高度变化的速率计算出蛋白离开珠进入溶液的速率。如果溶液中溶解有 BCA 的另一种小分子配体,则蛋白流出的速率会明显加快。本文开发了一个反应-扩散(RD)模型来解释这一观察结果以及其背后的物理有机化学。使用该模型,我们通过悬浮高度与时间的关系图,从 BCA 计算出几种未标记配体的解离常数。值得注意的是,尽管该方法不需要电,并且只需要一件廉价的设备,但它可以在广泛的解离常数范围内(在 10 nM 到 100 μM 的范围内)准确测量未标记蛋白与小分子的结合。使用该方法进行的测定通常可以在相对较短的时间内完成(20 分钟至 2 小时)。该系统的一个缺点是,在其目前的形式下,它不适用于分子量大于约 65 kDa 的蛋白质。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7c36/3433162/c2d721303b58/nihms390211f1.jpg

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