枸杞糖肽和异绿原酸A对RAW264.7细胞的协同免疫调节活性。
The synergistic immunomodulatory activity of Lycium barbarum glycopeptide and isochlorogenic acid A on RAW264.7 cells.
发表日期:2024 Oct 22
作者:
Ge Xu, Zhipeng Yu, Wenzhu Zhao
来源:
Food & Function
摘要:
调节免疫系统维持机体稳态已成为研究热点,多组分复合物的协同作用将有效提高免疫调节活性。本研究旨在探讨异绿原酸A(IAA)和枸杞糖肽(LbGp)的相互作用和协同免疫调节活性。结果表明,采用非共价分子间相互作用形成LbGp-IAA复合物,结合比例为135.15 mg g-1。 LbGp-IAA复合物的形成改变了LbGp的构象,IAA主要通过范德华力和氢键与LbGp结合。此外,LbGp-IAA促进RAW264.7细胞的增殖。 IAA与LbGp相互作用对促进吞噬作用以及一氧化氮、肿瘤坏死因子-α和白细胞介素-1β的表达具有协同作用,从而提高了LbGp的免疫调节作用。此外,LbGp和IAA的组合协同抑制脂多糖诱导的炎症反应。综上所述,IAA的结合增强了LbGp的免疫调节活性并协调免疫反应,并且不引发炎症反应,这可能归因于改变通过 IAA 的结合来研究 LbGp 的空间结构。该结果为糖肽-多酚相互作用的研究提供了新的视角。 © 2024 化学工业协会。© 2024 化学工业协会。
Regulation of the immune system to maintain homeostasis in the organism has become a focus of research, and the synergistic effect of multi-component complexes will effectively improve the immunomodulatory activity. The present study aimed to investigate the interaction and synergistic immunomodulatory activity of isochlorogenic acid A (IAA) and Lycium barbarum glycopeptide (LbGp).The results obtained indicated that non-covalent intermolecular interactions were employed to form the LbGp-IAA complex, with a binding ratio of 135.15 mg g-1. The formation of LbGp-IAA complex altered the conformation of LbGp, and IAA was mainly bound to LbGp by van der Waals forces and hydrogen bonds. In addition, LbGp-IAA promoted the proliferation of RAW264.7 cells. The IAA and LbGp interaction had a synergistic effect on the promotion of phagocytosis and the expression of nitric oxide, tumor necrosis faction-α and interleukin-1β, which improved the immunomodulatory effect of LbGp. Furthermore, the combination of LbGp and IAA synergistically inhibited lipopolysaccharide-induced inflammatory response.In summary, the binding of IAA enhanced the immunomodulatory activity of LbGp and coordinated the immune response, and did not trigger an inflammatory response, which was potentially attributed to the alteration of spatial structure of LbGp through the binding of IAA. The results provide new perspectives for the study of glycopeptide-polyphenol interactions. © 2024 Society of Chemical Industry.© 2024 Society of Chemical Industry.