Ren Jianhua, Sawhney Ashish, Tian Yuan, Padda Bhupinder, Batoon Patrick
Department of Chemistry, University of the Pacific.
J Vis Exp. 2013 Jun 24(76):4348. doi: 10.3791/4348.
Amino acid residues located at different positions in folded proteins often exhibit different degrees of acidities. For example, a cysteine residue located at or near the N-terminus of a helix is often more acidic than that at or near the C-terminus (1-6). Although extensive experimental studies on the acid-base properties of peptides have been carried out in the condensed phase, in particular in aqueous solutions (6-8), the results are often complicated by solvent effects (7). In fact, most of the active sites in proteins are located near the interior region where solvent effects have been minimized (9,10). In order to understand intrinsic acid-base properties of peptides and proteins, it is important to perform the studies in a solvent-free environment. We present a method to measure the acidities of oligopeptides in the gas-phase. We use a cysteine-containing oligopeptide, Ala3CysNH2 (A3CH), as the model compound. The measurements are based on the well-established extended Cooks kinetic method (Figure 1) (11-16). The experiments are carried out using a triple-quadrupole mass spectrometer interfaced with an electrospray ionization (ESI) ion source (Figure 2). For each peptide sample, several reference acids are selected. The reference acids are structurally similar organic compounds with known gas-phase acidities. A solution of the mixture of the peptide and a reference acid is introduced into the mass spectrometer, and a gas-phase proton-bound anionic cluster of peptide-reference acid is formed. The proton-bound cluster is mass isolated and subsequently fragmented via collision-induced dissociation (CID) experiments. The resulting fragment ion abundances are analyzed using a relationship between the acidities and the cluster ion dissociation kinetics. The gas-phase acidity of the peptide is then obtained by linear regression of the thermo-kinetic plots (17,18). The method can be applied to a variety of molecular systems, including organic compounds, amino acids and their derivatives, oligonucleotides, and oligopeptides. By comparing the gas-phase acidities measured experimentally with those values calculated for different conformers, conformational effects on the acidities can be evaluated.
位于折叠蛋白不同位置的氨基酸残基通常表现出不同程度的酸度。例如,位于螺旋N端或其附近的半胱氨酸残基通常比位于C端或其附近的半胱氨酸残基酸性更强(1 - 6)。尽管已经在凝聚相中,特别是在水溶液中对肽的酸碱性质进行了广泛的实验研究(6 - 8),但结果常常受到溶剂效应的影响而变得复杂(7)。实际上,蛋白质中的大多数活性位点位于内部区域附近,在该区域溶剂效应已被最小化(9,10)。为了理解肽和蛋白质的固有酸碱性质,在无溶剂环境中进行研究很重要。我们提出了一种在气相中测量寡肽酸度的方法。我们使用含半胱氨酸的寡肽Ala3CysNH2(A3CH)作为模型化合物。测量基于成熟的扩展库克斯动力学方法(图1)(11 - 16)。实验使用与电喷雾电离(ESI)离子源相连的三重四极杆质谱仪进行(图2)。对于每个肽样品,选择几种参考酸。参考酸是具有已知气相酸度的结构相似的有机化合物。将肽和参考酸的混合物溶液引入质谱仪,形成肽 - 参考酸的气相质子结合阴离子簇。对质子结合簇进行质量分离,随后通过碰撞诱导解离(CID)实验进行碎片化。使用酸度与簇离子解离动力学之间的关系分析所得碎片离子丰度。然后通过热动力学图的线性回归获得肽的气相酸度(17,18)。该方法可应用于多种分子系统,包括有机化合物、氨基酸及其衍生物、寡核苷酸和寡肽。通过将实验测量的气相酸度与针对不同构象计算的值进行比较,可以评估酸度的构象效应。