Molecular interactions between soybean glycinin (11S) and genistin: Impact of glycosylation

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids Pub Date : 2025-02-24 DOI:10.1016/j.foodhyd.2025.111266

Emelia Smith , Lloyd Condict , John Ashton , Stefan Kasapis

{"title":"Molecular interactions between soybean glycinin (11S) and genistin: Impact of glycosylation","authors":"Emelia Smith , Lloyd Condict , John Ashton , Stefan Kasapis","doi":"10.1016/j.foodhyd.2025.111266","DOIUrl":null,"url":null,"abstract":"<div><div>The nature of molecular interactions between soy glycinin (11S) and genistin (GNI) at near neutral pH and ambient temperature was investigated using molecular dynamics and a variety of spectroscopic methods to understand the impact of isoflavone glycosylation. Fluorescence quenching in combination with a Job plot analysis predicted that GNI binds to a single trimer of the 11S molecule in a 1:1 ratio with a binding affinity (K<sub>A</sub>) of 1.05 × 10<sup>5</sup> M<sup>−1</sup>. Secondary structure analysis by circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) revealed GNI did not cause any significant structural alterations to the protein following complexation. UV–vis measurements did not show any changes in absorption of 11S in the presence of GNI, suggesting that interactions were non-covalent in nature. These findings were confirmed by molecular docking and dynamics whereby the top-ranking binding site revealed GNI was stabilised in the interior hydrophobic region of 11S by 5 persistent hydrogen bonds from 11S and hydroxyl groups of the GNI glucoside. In contrast, in silico modelling from this work on the aglycone counterpart, genistein (GNE), exhibited a less stable, more dynamic behaviour, with fleeting hydrogen bond formation, consistent with a lower binding affinity/association with 11S. Overall, phenolic glycosylation significantly increased the ligand binding affinity and stability with soy 11S due to additional hydroxyl groups on the glucoside participating in persistent hydrogen bonds.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"165 ","pages":"Article 111266"},"PeriodicalIF":11.0000,"publicationDate":"2025-02-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Hydrocolloids","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0268005X25002267","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}

引用次数: 0

Abstract

The nature of molecular interactions between soy glycinin (11S) and genistin (GNI) at near neutral pH and ambient temperature was investigated using molecular dynamics and a variety of spectroscopic methods to understand the impact of isoflavone glycosylation. Fluorescence quenching in combination with a Job plot analysis predicted that GNI binds to a single trimer of the 11S molecule in a 1:1 ratio with a binding affinity (K_A) of 1.05 × 10⁵ M⁻¹. Secondary structure analysis by circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) revealed GNI did not cause any significant structural alterations to the protein following complexation. UV–vis measurements did not show any changes in absorption of 11S in the presence of GNI, suggesting that interactions were non-covalent in nature. These findings were confirmed by molecular docking and dynamics whereby the top-ranking binding site revealed GNI was stabilised in the interior hydrophobic region of 11S by 5 persistent hydrogen bonds from 11S and hydroxyl groups of the GNI glucoside. In contrast, in silico modelling from this work on the aglycone counterpart, genistein (GNE), exhibited a less stable, more dynamic behaviour, with fleeting hydrogen bond formation, consistent with a lower binding affinity/association with 11S. Overall, phenolic glycosylation significantly increased the ligand binding affinity and stability with soy 11S due to additional hydroxyl groups on the glucoside participating in persistent hydrogen bonds.

Abstract Image

查看原文本刊更多论文

求助全文

约1分钟内获得全文求助全文

来源期刊

Food Hydrocolloids 工程技术-食品科技

CiteScore

19.90

自引率

14.00%

发文量

871

审稿时长

37 days

期刊介绍： Food Hydrocolloids publishes original and innovative research focused on the characterization, functional properties, and applications of hydrocolloid materials used in food products. These hydrocolloids, defined as polysaccharides and proteins of commercial importance, are added to control aspects such as texture, stability, rheology, and sensory properties. The research's primary emphasis should be on the hydrocolloids themselves, with thorough descriptions of their source, nature, and physicochemical characteristics. Manuscripts are expected to clearly outline specific aims and objectives, include a fundamental discussion of research findings at the molecular level, and address the significance of the results. Studies on hydrocolloids in complex formulations should concentrate on their overall properties and mechanisms of action, while simple formulation development studies may not be considered for publication. The main areas of interest are: -Chemical and physicochemical characterisation Thermal properties including glass transitions and conformational changes- Rheological properties including viscosity, viscoelastic properties and gelation behaviour- The influence on organoleptic properties- Interfacial properties including stabilisation of dispersions, emulsions and foams- Film forming properties with application to edible films and active packaging- Encapsulation and controlled release of active compounds- The influence on health including their role as dietary fibre- Manipulation of hydrocolloid structure and functionality through chemical, biochemical and physical processes- New hydrocolloids and hydrocolloid sources of commercial potential. The Journal also publishes Review articles that provide an overview of the latest developments in topics of specific interest to researchers in this field of activity.