Details

Autor(en) / Beteiligte

• Zhao, Xingyu
• Chai, Zhi
• Wang, Jing
• Hou, Dongjie
• Li, Bin
• Zhang, Lixia
• Huang, Wuyang

Titel

Assessment on malvidin-3-glucoside interaction with TLR4 via multi-spectroscopic analysis and molecular docking

Ist Teil von

• Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 2024-10, Vol.318, p.124460, Article 124460

Ort / Verlag

Elsevier B.V

Erscheinungsjahr

2024

Link zum Volltext

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• [Display omitted] •Mv-3-glc could quench the intrinsic fluorescence of TLR4.•The interaction of Mv-3-glc with TLR4 is forming a stable complex.•Hydrogen bonding and van der Waals' force were both important interaction forces.•Mv-3-glc bound to TLR4/MD-2′s hydrophobic pocket at sites Phe126, Ser127, etc.•Blueberry anthocyanins might regulate glucolipid metabolism by targeting to TLR4. As one innate immune pattern recognition receptor, Toll-like receptor 4 (TLR4) recently has been considered as a critical player in glucolipid metabolism. Blueberries contain high level of anthocyanins, especially malvidin-3-glucoside (Mv-3-glc), which contribute the anti-inflammatory, hypoglycemic, and hypolipidemic effects. It is speculated that Mv-3-glc is able to possess these functions by binding to TLR4. Here, the noncovalent interactions of Mv-3-glc and TLR4 was explored through multi-techniques including fluorescence and ultraviolet–visible (UV–Vis) absorption spectroscopy, as well as molecular docking. The results demonstrated that Mv-3-glc was able to quench TLR4 intrinsic fluorescence effectively. A stable complex was formed spontaneously and the reaction was exothermic. The degree of binding of Mv-3-glc to TLR4 showed a strong dependence on the chemical concentration, temperature, and pH values. The negative signs for enthalpy (ΔH = -69.1 ± 10.8 kJ/mol) and entropy (ΔS = -105.0 ± 12.3 J/mol/K) from the interaction of the Mv-3-glc and TLR4 shows that the major driving forces are the hydrogen bonding and van der Waals' force, which is consistent with the molecular docking results. In addition, molecular docking predicted that the active center with specific amino acid residues, Phe126, Ser127, Leu54, Ile153, and Tyr131 was responsible for the site of Mv-3-glc binding to TLR4/myeloid differentiation protein-2 (MD-2). These findings confirmed that Mv-3-glc could bind to TLR4, which would be beneficial to understand the target therapeutic effects of blueberry anthocyanins on TLR4 in regulating glucolipid metabolism.