Volume 14 Issue 7
Jul.  2024
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Hongna Su, Lili He, Xina Yu, Yue Wang, Li Yang, Xiaorui Wang, Xiaojun Yao, Pei Luo, Zhifeng Zhang. Structural characterization and mechanisms of macrophage immunomodulatory activity of a novel polysaccharide with a galactose backbone from the processed Polygonati Rhizoma[J]. Journal of Pharmaceutical Analysis, 2024, 14(7): 100974. doi: 10.1016/j.jpha.2024.100974
Citation: Hongna Su, Lili He, Xina Yu, Yue Wang, Li Yang, Xiaorui Wang, Xiaojun Yao, Pei Luo, Zhifeng Zhang. Structural characterization and mechanisms of macrophage immunomodulatory activity of a novel polysaccharide with a galactose backbone from the processed Polygonati Rhizoma[J]. Journal of Pharmaceutical Analysis, 2024, 14(7): 100974. doi: 10.1016/j.jpha.2024.100974

Structural characterization and mechanisms of macrophage immunomodulatory activity of a novel polysaccharide with a galactose backbone from the processed Polygonati Rhizoma

doi: 10.1016/j.jpha.2024.100974
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This work was supported by Sichuan Provincial Regional Innovation Cooperation Project, China (Grant No.: 2023YFQ0084) and the Macau Science and Technology Development Fund (FDCT), China (Grant No.: 0043/2021/AGJ).

  • Received Date: Sep. 21, 2023
  • Accepted Date: Mar. 28, 2024
  • Rev Recd Date: Feb. 05, 2024
  • Publish Date: Mar. 29, 2024
  • A purified polysaccharide with a galactose backbone (SPR-1, Mw 3,622 Da) was isolated from processed Polygonati Rhizoma with black beans (PRWB) and characterized its chemical properties. The backbone of SPR-1 consisted of [(4)-β-D-Galp-(1]9 → 4,6)-β-D-Galp-(1 → 4)-α-D-GalpA-(1 → 4)-α-D-GalpA-(1 → 4)-α-D-Glcp-(1 → 4,6)-α-D-Glcp-(1 → 4)-α/β-D-Glcp, with a branch chain of R1: β-D-Galp-(1 → 3)-β-D-Galp-(1→ connected to the →4,6)-β-D-Galp-(1→ via O-6, and a branch chain of R2: α-D-Glcp-(1 → 6)-α-D-Glcp-(1→ connected to the →4,6)-α-D-Glcp-(1→ via O-6. Immunomodulatory assays showed that the SPR-1 significantly activated macrophages, and increased secretion of NO and cytokines (i.e., IL-1β and TNF-α), as well as promoted the phagocytic activities of cells. Furthermore, isothermal titration calorimetry (ITC) analysis and molecular docking results indicated high-affinity binding between SPR-1 and MD2 with the equilibrium dissociation constant (KD) of 18.8 μM. It was suggested that SPR-1 activated the immune response through Toll-like receptor 4 (TLR4) signaling and downstream responses. Our research demonstrated that the SPR-1 has a promising candidate from PRWB for the TLR4 agonist to induce immune response, and also provided an easily accessible way that can be used for PR deep processing.

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