Ahmed Taha , Federico Casanova , Ibrahim Khalifa , Martynas Talaikis , Monika Kirsnytė , Arūnas Stirkė
{"title":"BSA/EGCG binding affinity modified by nanosecond pulsed electric field","authors":"Ahmed Taha , Federico Casanova , Ibrahim Khalifa , Martynas Talaikis , Monika Kirsnytė , Arūnas Stirkė","doi":"10.1016/j.foodhyd.2025.111184","DOIUrl":null,"url":null,"abstract":"<div><div>The effects of nanosecond pulsed electric field (nsPEF) on the structure of bovine serum albumin (BSA) and its binding with epigallocatechin gallate (EGCG) were investigated. nsPEF (0–20 kV/cm, 90 ns, 1–3 pulses) was applied to both BSA alone and BSA/EGCG mixtures. Multispectral, namely circular dichroism (CD), ultraviolet (UV–vis), fluorescence, Fourier Transform Infrared (FTIR), Raman spectroscopy, and dynamic light scattering (DLS), alongside with the molecular modeling docking methods were employed in this study to confirm the degree of BSA/EGCG interaction. Results revealed that nsPEF (16 kV/cm) increased the particle size of BSA from 23.8 to 39.4 nm, where the ζ-potential value varied from −10.1 to −28.9 mV. CD showed that nsPEF treatment improved the α-helix but decreased the β-turns and unordered structures. Adding EGCG to nsPEF-induced BSA caused a significant increase in BSA particle sizes and a decline in surface hydrophobicity and fluorescence intensity. Moreover, when nsPEF was applied to BSA/EGCG mixtures, the particle size of BSA rose from 21.3 nm (before treatment) to 69.6 nm after treatment at 8 kV/cm. Raman spectroscopy results confirmed that nsPEF treatment-induced changes in BSA structure in S-S and S-C bonds. Changes in amide Ι and Ⅱ were also observed in FTIR spectra of nsPEF-induced BSA/EGCG mixtures. Molecular docking confirmed that BSA can bind with EGCG via H-bonds at specific active sites on both molecules. In conclusion, nsPEF, as a green technology, can be utilized successfully to alter BSA structure and facilitate BSA/EGCG binding.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"164 ","pages":"Article 111184"},"PeriodicalIF":11.0000,"publicationDate":"2025-02-06","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/S0268005X25001444","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 effects of nanosecond pulsed electric field (nsPEF) on the structure of bovine serum albumin (BSA) and its binding with epigallocatechin gallate (EGCG) were investigated. nsPEF (0–20 kV/cm, 90 ns, 1–3 pulses) was applied to both BSA alone and BSA/EGCG mixtures. Multispectral, namely circular dichroism (CD), ultraviolet (UV–vis), fluorescence, Fourier Transform Infrared (FTIR), Raman spectroscopy, and dynamic light scattering (DLS), alongside with the molecular modeling docking methods were employed in this study to confirm the degree of BSA/EGCG interaction. Results revealed that nsPEF (16 kV/cm) increased the particle size of BSA from 23.8 to 39.4 nm, where the ζ-potential value varied from −10.1 to −28.9 mV. CD showed that nsPEF treatment improved the α-helix but decreased the β-turns and unordered structures. Adding EGCG to nsPEF-induced BSA caused a significant increase in BSA particle sizes and a decline in surface hydrophobicity and fluorescence intensity. Moreover, when nsPEF was applied to BSA/EGCG mixtures, the particle size of BSA rose from 21.3 nm (before treatment) to 69.6 nm after treatment at 8 kV/cm. Raman spectroscopy results confirmed that nsPEF treatment-induced changes in BSA structure in S-S and S-C bonds. Changes in amide Ι and Ⅱ were also observed in FTIR spectra of nsPEF-induced BSA/EGCG mixtures. Molecular docking confirmed that BSA can bind with EGCG via H-bonds at specific active sites on both molecules. In conclusion, nsPEF, as a green technology, can be utilized successfully to alter BSA structure and facilitate BSA/EGCG binding.
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.