The Investigation of β‐Cyclodextrin Noncovalent Complex with Protein or Dipeptide by Electrospray Ionization Mass Spectrometry

Abstract

Electrospray ionization ion trap mass spectrometry was used for the investigation of noncovalent complexes formed between β‐cyclodextrin (CD) and protein or dipeptide in aqueous solution. After one of those noncovalent complexes has formed, it was found that addition of the other ligand compound would produce the competitive noncovalent complexes. Measurements were obtained with four proteins, such as hen egg lysozyme, cytochrome c, insulin and RNase A, and three dipeptides, respectively. The data obtained from the investigated systems show that ESI‐MS is not only a reliable, sensitive, and fast technique for the analysis of the β‐CD/protein and β‐CD/dipeptide complexes, but also an interesting tool to observe the transformation from one complex to the other in aqueous solution.

Keywords:

• β‐Cyclodextrin
• Noncovalent interactions
• Cytochrome c
• Lysozyme

Acknowledgments

The authors would like to acknowledge the financial supports from the Chinese National Natural Science Foundation (No. 20175026), the Chinese Ministry of Education and Zhengzhou University.