From Langmuir films to molecular docking: unraveling the interfacial code of (-)-epigallocatechin gallate binding with milk fat globule membrane components

  • Food Res Int. 2026 Sep 1:239:119529. doi: 10.1016/j.foodres.2026.119529.
Xingyi Li  1 ,  Yajuan Li  1 ,  Wei Mao  1 ,  Hui Zhou  2 ,  Xiankang Fan  1 ,  Zhonghua Liu  3 ,  Maiquan Li  4 ,  Jie Luo  5
Affiliations
  • 1. College of Food Science and Technology, Hunan Agricultural University, Changsha 410114, China.
  • 2. College of Food Science and Technology, Hunan Agricultural University, Changsha 410114, China. Electronic address: [email protected].
  • 3. College of Horticulture, Hunan Agricultural University, 410128 Changsha, China. Electronic address: [email protected].
  • 4. College of Food Science and Technology, Hunan Agricultural University, Changsha 410114, China. Electronic address: [email protected].
  • 5. College of Food Science and Technology, Hunan Agricultural University, Changsha 410114, China. Electronic address: [email protected].
PMID: 42270243 DOI: 10.1016/j.foodres.2026.119529
Abstract

This study investigated the interaction mechanisms between epigallocatechin gallate (EGCG) and key milk fat globule membrane (MFGM) components, aiming to elucidate the basis for MFGM-catechin interactions. Initial evidence from 1H and 31P NMR spectroscopy revealed EGCG-induced chemical shifts in critical regions. Furthermore, Langmuir monolayer studies simulating MFGM demonstrated concentration-dependent interactions of EGCG with the membrane interface. A significant reduction in the collapse pressure of sphingomyelin monolayers (from 43.84 ± 2.58 mN/m to 27.41 ± 3.06 mN/m) provided direct evidence of strong EGCG-phospholipid binding. Atomic force microscopy (AFM) further corroborated these interactions, indicating EGCG-induced lipid aggregation and protein structural alterations. Fourier transform infrared (FTIR) spectroscopy, molecular docking, and molecular dynamics simulations identified hydrogen bonding and hydrophobic interactions as the primary driving forces for these phenomena. Overall, these results elucidate the molecular mechanisms underpinning EGCG-MFGM component interactions, providing a foundational understanding for leveraging MFGM constituents to alleviate EGCG-related astringency in food applications.

Keywords
Epigallocatechin Gallate; Langmuir monolayer; Milk fat globule membrane; Molecular interactions; Phospholipids.
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