Quantitative Proteomics Combined with Affinity MS Revealed the Molecular Mechanism of Ginsenoside Antitumor Effects

• DOI: 10.1021/acs.jproteome.8b00972
• Publication Date: 2019-03-12T16:36:09Z
• Authors: Zhihua Wang; Unchol Kim; Yanting Jiao; Chaowen Li; Yingying Guo; Xiaoyao Ma; Min Jiang; Zhihong Jiang; Yuanyuan Hou; Gang Bai
• Keywords: Protopanaxadiol

Ginsenosides have previously been demonstrated to effectively inhibit cancer cell growth and survival in both animal models lines. However, the specific ginsenoside component that is active ingredient for treatment through interaction with a target protein remains unknown. By an integrated quantitative proteomics approach via affinity mass spectrum (MS) technology, we deciphered core structure of derived from crude extracts ginsenosides progressed toward identifying mediates its anticancer activity. The Tandem Mass Tag (TMT) labeling technique acquired 55620 MS/MS spectra identified 5499 proteins 3045 modified proteins. Of these proteins, 224 differentially expressed were significantly altered nonsmall lung Bioinformatics tools comprehensive analysis revealed Ras played general regulatory role many functional pathways was probably direct compound ginsenosides. Then, MS screening based on 20(s)-protopanaxadiol, 20(s)-Ginsenoside Rh2, Rg3 had under different conditions. In particular, whose derivatives are reported antitumor compounds Rh2 higher low KD 1.22 μM mutation sites G12 G60, play those interactions. Moreover, molecular mechanism bioactivity assessment results confirmed identity chemical ligand directly acting GTP binding pocket shown be effective profiles.