TY - JOUR
T1 - BSA/EGCG binding affinity modified by nanosecond pulsed electric field
AU - Taha, Ahmed
AU - Casanova, Federico
AU - Khalifa, Ibrahim
AU - Talaikis, Martynas
AU - Kirsnytė, Monika
AU - Stirkė, Arūnas
PY - 2025
Y1 - 2025
N2 - 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.
AB - 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.
KW - BSA
KW - EGCG
KW - Nanosecond pulsed electric field
KW - Binding
KW - Mechanism
U2 - 10.1016/j.foodhyd.2025.111184
DO - 10.1016/j.foodhyd.2025.111184
M3 - Journal article
SN - 0268-005X
VL - 164
JO - Food Hydrocolloids
JF - Food Hydrocolloids
M1 - 111184
ER -