Structural modification of lactoferrin by epigallocatechin gallate: elucidation of its structure and exploration of its potential in promoting osteoblast proliferation.
{"title":"Structural modification of lactoferrin by epigallocatechin gallate: elucidation of its structure and exploration of its potential in promoting osteoblast proliferation.","authors":"Zhenni Zhai, Xiaoni Lian, Fengjiao Fan, Peng Li, Jian Ding, Xinyang Sun, Xiaoyi Jiang, Ziqian Li, Yong Fang","doi":"10.1039/d4fo05973e","DOIUrl":null,"url":null,"abstract":"<p><p>Lactoferrin (LF) and epigallocatechin gallate (EGCG) are recognized for their potent osteogenic properties. However, the osteogenic activity of LF-EGCG complexes is not fully understood. In this study, both non-covalent and covalent LF-EGCG complexes with different LF : EGCG ratios were prepared, and their effects on the LF structure and thermal stability were investigated using circular dichroism, Fourier transform infrared spectroscopy, fluorescence spectroscopy, Raman spectroscopy, and differential scanning calorimetry. The results indicated that covalent binding had a more pronounced effect on protein structure modification. The covalent complex with an LF : EGCG ratio of 5 : 1 demonstrated maximum hydrophilicity; the particle size reduced to 19.31 nm; and the denaturation temperature increased to 56.96 °C. This complex at a 100 μg mL<sup>-1</sup> concentration significantly enhanced osteoblast proliferation, increasing the rate to 1.34-fold. The proliferation rate of osteoblasts was significantly correlated with the tyrosine residue microenvironment and hydrophobicity of the complexes. This study provides valuable insights and strategies for enhancing the nutritional efficacy of LF.</p>","PeriodicalId":77,"journal":{"name":"Food & Function","volume":" ","pages":""},"PeriodicalIF":5.1000,"publicationDate":"2025-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food & Function","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1039/d4fo05973e","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Lactoferrin (LF) and epigallocatechin gallate (EGCG) are recognized for their potent osteogenic properties. However, the osteogenic activity of LF-EGCG complexes is not fully understood. In this study, both non-covalent and covalent LF-EGCG complexes with different LF : EGCG ratios were prepared, and their effects on the LF structure and thermal stability were investigated using circular dichroism, Fourier transform infrared spectroscopy, fluorescence spectroscopy, Raman spectroscopy, and differential scanning calorimetry. The results indicated that covalent binding had a more pronounced effect on protein structure modification. The covalent complex with an LF : EGCG ratio of 5 : 1 demonstrated maximum hydrophilicity; the particle size reduced to 19.31 nm; and the denaturation temperature increased to 56.96 °C. This complex at a 100 μg mL-1 concentration significantly enhanced osteoblast proliferation, increasing the rate to 1.34-fold. The proliferation rate of osteoblasts was significantly correlated with the tyrosine residue microenvironment and hydrophobicity of the complexes. This study provides valuable insights and strategies for enhancing the nutritional efficacy of LF.
期刊介绍:
Food & Function provides a unique venue for physicists, chemists, biochemists, nutritionists and other food scientists to publish work at the interface of the chemistry, physics and biology of food. The journal focuses on food and the functions of food in relation to health.