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Study of the non‐covalent interactions of ginsenosides and lysozyme using electrospray ionization mass spectrometry
Author(s) -
Tang Jun,
Fu Qiang,
Cui Meng,
Xing Junpeng,
Liu Zhiqiang,
Liu Shuying
Publication year - 2015
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.7366
Subject(s) - chemistry , electrospray ionization , chromatography , lysozyme , mass spectrometry , extractive electrospray ionization , electrospray , direct electron ionization liquid chromatography–mass spectrometry interface , ionization , protein mass spectrometry , analytical chemistry (journal) , chemical ionization , organic chemistry , ion , biochemistry
Rationale Ginsenosides are an important class of natural products extracted from ginseng that possess various important biological activities. Studies of interactions of ginsenosides with proteins are essential for comprehensive understanding of the biological activities of ginsenosides. In this study, the interactions of ginsenosides with lysozyme were investigated by electrospray ionization mass spectrometry (ESI‐MS). Methods Both protopanaxadiol‐type and protopanaxatriol‐type ginsenosides were chosen to explore the interactions of ginsenosides towards lysozyme near the physiological conditions by direct ESI‐MS, respectively. Comparative experiments were conducted to confirm the interactions were specific. In addition, the dissociation constants of ginsenoside‐lysozyme complexes were determined by a ESI‐MS titration strategy. Results The results showed ginsenosides bound to lysozyme at the stoichiometries of 1:1 and 2:1. The association constants of ginsenosides to lysozyme were in the order of Re>Rd>Rf>Rg 2 >Rg 3 . According to their structures, the binding affinities associated with the type of aglycone and the type and the number of sugar moieties linked on the aglycone. Conclusions It has been demonstrated that ESI‐MS is a powerful tool to probe the non‐covalent interactions between lysozyme and ginsenosides. These results provide insights into the interaction of ginsenosides with lysozyme at the molecular level. The developed strategy could be applied to determine the interactions of proteins with other natural products. Copyright © 2015 John Wiley & Sons, Ltd.