Influence of Alkylammonium Acetate Buffers on Protein–Ligand Noncovalent Interactions Using Native Mass Spectrometry

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• 作者：Xiaoyu Zhuang ; Agni F. M. Gavriilidou…
• 关键词：Noncovalent interactions ; Alkylammonium salts ; Charge reduction ; Native mass spectrometry
• 刊名：Journal of The American Society for Mass Spectrometry
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：28
• 期：2
• 页码：341-346
• 全文大小：
• 刊物主题：Analytical Chemistry; Biotechnology; Organic Chemistry; Proteomics; Bioinformatics;
• 出版者：Springer US
• ISSN：1879-1123
• 卷排序：28

文摘

We investigate the influence of three volatile alkylammonium acetate buffers on binding affinities for protein–ligand interactions determined by native electrospray ionization-mass spectrometry (ESI-MS). Four different types of proteins were chosen for this study. A charge-reduction effect was observed for all the cases studied, in comparison to the ions formed in ammonium acetate solution. When increasing the collision energy, the complexes of trypsin and the ligand were found to be more stable when sprayed from alkylammonium acetate buffers than from ammonium acetate. The determined dissociation constant (K_d) also exhibited a drop (up to 40%) when ammonium acetate was replaced by alkylammonium acetate buffers for the case of lysozyme and the ligand. The prospective uses of these ammonium acetate analogs in native ESI-MS are discussed in this paper as well.