Lengqvist Johan, Alvélius Gunvor, Jörnvall Hans, Sjövall Jan, Perlmann Thomas, Griffiths William J
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
J Am Soc Mass Spectrom. 2005 Oct;16(10):1631-40. doi: 10.1016/j.jasms.2005.06.003.
Accurate mass measurements are often used in the structural determination of unknown compounds of low molecular mass (i.e., below approximately 500 Da). Recently, it has been shown that accurate mass measurements also can be made on small denatured proteins (i.e., M(r), approximately 17,000) to confirm their amino acid composition and identify the presence of isoforms. In the current report, we present nondenaturing electrospray (ES) mass spectrometry data on the direct accurate mass measurement of ligands in complex with the retinoid X receptor ligand binding domain (RXR LBD; M(r) 31,370.92). Average mass errors were below 0.198 Da, 6.3 ppm (standard deviation [SD], 0.146; n = 10) for low-affinity fatty acid agonists analyzed in complex with the RXR LBD. Protein consumption was less than 15 pmol, with fatty acid ligands present at concentrations corresponding to their median effective concentration value (low micromolar, determined in transfection assays). Although determination of fatty acid mass was only sufficiently accurate to give nominal mass values, measurements were of sufficient accuracy to assign fatty acid chain length, degree of unsaturation, or cyclization. Using 17beta-estradiol as a control, the ability to observe specific ligand binding is shown for both high- and low-affinity RXRalpha agonists. In addition, binding of a novel synthetic receptor agonist XCT0315908 to the RXRalpha LBD is reported. This compound showed a high degree of complex formation, and the receptor-ligand complex could be mass measured with an average mass error of -0.024 Da, 0.8 ppm (SD, 0.092; n = 9). Thus, specific binding of both nanomolar and micromolar affinity ligands to a nuclear receptor LBD can be directly observed using nondenaturing ES mass spectrometry and accurate mass measurements additionally can be made on intact complexes in the same experiment. This methodology also is applicable when ligands are present as components of mixtures.
精确质量测量常用于低分子量未知化合物(即分子量低于约500 Da)的结构测定。最近有研究表明,精确质量测量也可用于对小的变性蛋白质(即分子量约为17,000)进行分析,以确认其氨基酸组成并鉴定异构体的存在。在本报告中,我们展示了非变性电喷雾(ES)质谱数据,用于直接精确测量与视黄酸X受体配体结合域(RXR LBD;分子量31,370.92)结合的配体。对于与RXR LBD结合分析的低亲和力脂肪酸激动剂,平均质量误差低于0.198 Da,6.3 ppm(标准差[SD],0.146;n = 10)。蛋白质消耗量小于15 pmol,脂肪酸配体的浓度对应于其半数有效浓度值(低微摩尔浓度,在转染实验中测定)。尽管脂肪酸质量的测定仅足够精确以给出标称质量值,但测量精度足以确定脂肪酸链长度、不饱和度或环化程度。以17β - 雌二醇作为对照,展示了高亲和力和低亲和力RXRα激动剂观察特异性配体结合的能力。此外,还报道了一种新型合成受体激动剂XCT0315908与RXRα LBD的结合。该化合物显示出高度的复合物形成,并且受体 - 配体复合物的质量测量平均质量误差为 -0.024 Da,0.8 ppm(SD,0.092;n = 9)。因此,使用非变性ES质谱可以直接观察到纳摩尔和微摩尔亲和力配体与核受体LBD的特异性结合,并且在同一实验中还可以对完整复合物进行精确质量测量。当配体作为混合物的成分存在时,这种方法同样适用。