期刊
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
卷 32, 期 6, 页码 1530-1537出版社
AMER CHEMICAL SOC
DOI: 10.1021/jasms.1c00130
关键词
-
资金
- MOST [102-2113M-001-002-MY5MOST, 103-2325-B-001-014]
- Genomics Research Center, Academia Sinica in Taiwan [NHRIEX104-10301EI]
- The Scientific Research Commission (BAPK) of Sakarya University in Turkey
In this study, it was observed that Ag(I) ions effectively form stable Ag(I)(1-4)-insulin complexes with high formation equilibrium constants.
Ag(I)-insulin complex formation was investigated using electrospray quadrupole ion trap mass spectrometry (ESI-QIT-MS), and Ag(I) ion binding to an insulin molecule was evaluated. The Ag(I) binding ratios were measured in the range of pH 3-8. The highest binding ratio of the Ag(I) ions was obtained at pH 7. Spectrometric titration was carried out at varied molar ratios of Ag(I) ions to insulin from 20/1 to 250/1. It was observed that four Ag(I) ions were bound effectively to an insulin molecule to form Ag(I)(1-4)-insulin complexes. The formation equilibrium constants of Ag(I)(1-4)-insulin complexes were calculated from the ESI-QIT-MS peak intensities. The equilibrium constants were found as K-f1 = (2.92 +/- 0.18) x 10(4) M-1, K-f2 = (1.03 +/- 0.07) x 10(4) M-1, K-f3 = (6.67 +/- 0.46) x 10(3) M-1, and K-f4 = (2.00 +/- 0.16) x 10(3) M-1. The tandem MS/MS spectroscopies were studied to evaluate the stability of the Ag(I) complexes. The different flow rates with nano-ESI were performed to determine the binding of Ag(I) ions in solution or gas phase. In conclusion, it was observed that the Ag(I) ion forms stable Ag(I)(1-4)-complexes with high formation equilibrium constants.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据