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Biomolecules
Volume 16
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10.3390/biom16081153
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This is an early access version, the complete PDF, HTML, and XML versions will be available soon.
Article

Molecular Interactions and Antioxidant Properties of White Wine Phytochemicals: A Mechanistic Study of Serum Protein Binding

by
Dinorah Barasch
1,
Alina Nemirovski
1,
Emmanuelle Merquiol
1,
Joseph Deutsch
1,*,
Dejian Huang
2,
Pitipong Thobunluepop
3,
Alma Leticia Martinez-Ayala
4,
Patricia Arancibia-Avila
5,
Fernando Toledo-Montiel
5,
Paweł Paśko
6 and
Shela Gorinstein
1,*
1
Institute for Drug Research, School of Pharmacy, Faculty of Medicine, The Hebrew University of Jerusalem, Jerusalem 9112001, Israel
2
Department of Food Science & Technology, National University of Singapore, Singapore 117542, Singapore
3
Department of Agronomy, Faculty of Agriculture, Kasetsart University, Chatuchak, Bangkok 10900, Thailand
4
Centro de Desarrollo de Productos Bióticos, Instituto Politécnico Nacional, Yautepec 62731, Morelos, Mexico
5
Departamento de Ciencias Básicas, Facultad de Ciencias, Universidad del Bío-Bío, Chillán 378 000, Chile
6
Department of Food Chemistry and Nutrition, Faculty of Pharmacy, Jagiellonian University Medical College, 30-688 Kraków, Poland
*
Authors to whom correspondence should be addressed.
Biomolecules 2026, 16(8), 1153; https://doi.org/10.3390/biom16081153
Submission received: 7 July 2026 / Revised: 1 August 2026 / Accepted: 4 August 2026 / Published: 7 August 2026
(This article belongs to the Special Issue Phytochemicals: Bioactivity in Disease Prevention, Anti-Inflammation, and Animal/Human Health)
Versions Notes

Abstract

This study investigated the interactions between phenolic compounds from Israeli and Chilean white wines and human serum carrier proteins, including human serum albumin (HALB), gamma-globulin (HGLO), and fibrinogen (HFB), to characterize their antioxidant capacity and serum protein-binding behavior under controlled experimental conditions. The analyzed wines included Israeli Chardonnay (ICR), Chilean Chardonnay (CCR), Israeli Sauvignon Blanc (ISB), and Chilean Sauvignon Blanc (CSB). HPLC and FTIR fingerprinting revealed cultivar- and region-dependent differences in phenolic composition, with Chardonnay wines showing stronger protein-binding behavior and Sauvignon Blanc samples displaying high antioxidant efficiency relative to their phenolic content. ICR exhibited the highest total binding capacity, 46.44%, and the strongest albumin interaction, with a binding constant (Kb) of 8.44 × 104 M−1 and a Gibbs free energy (ΔG) value of −35.03 kJ/mol. Empirical fluorescence quenching kinetics demonstrated that white wine phenolics establish stable physical complexes with human serum proteins, displaying a distinct preferential affinity for HALB as the protein showing the strongest apparent interaction among the proteins tested. Two- and three-dimensional fluorescence spectroscopy confirmed substantial quenching of the intrinsic tryptophan and tyrosine residues, indicating meaningful microenvironmental alterations within the protein’s active transport sites. These empirical interactions were closely mirrored by complementary molecular docking simulations, which provided a structural visualization of the physical binding interactions. ICR also showed the highest antioxidant capacity, with DPPH and CUPRAC values of 1.66 and 2.91 mmol TE/L, respectively. Ethanol control showed negligible effects, indicating that the observed bioactivity was mainly associated with the polyphenolic matrix. Among the investigated samples, Chardonnay showed higher apparent protein-binding capacity, whereas Sauvignon Blanc showed relatively high antioxidant efficiency in relation to its phenolic content.
Keywords: human serum albumin; white wine phenolics; molecular docking; polyphenol-protein interaction; fluorescence quenching human serum albumin; white wine phenolics; molecular docking; polyphenol-protein interaction; fluorescence quenching

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MDPI and ACS Style

Barasch, D.; Nemirovski, A.; Merquiol, E.; Deutsch, J.; Huang, D.; Thobunluepop, P.; Martinez-Ayala, A.L.; Arancibia-Avila, P.; Toledo-Montiel, F.; Paśko, P.; et al. Molecular Interactions and Antioxidant Properties of White Wine Phytochemicals: A Mechanistic Study of Serum Protein Binding. Biomolecules 2026, 16, 1153. https://doi.org/10.3390/biom16081153

AMA Style

Barasch D, Nemirovski A, Merquiol E, Deutsch J, Huang D, Thobunluepop P, Martinez-Ayala AL, Arancibia-Avila P, Toledo-Montiel F, Paśko P, et al. Molecular Interactions and Antioxidant Properties of White Wine Phytochemicals: A Mechanistic Study of Serum Protein Binding. Biomolecules. 2026; 16(8):1153. https://doi.org/10.3390/biom16081153

Chicago/Turabian Style

Barasch, Dinorah, Alina Nemirovski, Emmanuelle Merquiol, Joseph Deutsch, Dejian Huang, Pitipong Thobunluepop, Alma Leticia Martinez-Ayala, Patricia Arancibia-Avila, Fernando Toledo-Montiel, Paweł Paśko, and et al. 2026. "Molecular Interactions and Antioxidant Properties of White Wine Phytochemicals: A Mechanistic Study of Serum Protein Binding" Biomolecules 16, no. 8: 1153. https://doi.org/10.3390/biom16081153

APA Style

Barasch, D., Nemirovski, A., Merquiol, E., Deutsch, J., Huang, D., Thobunluepop, P., Martinez-Ayala, A. L., Arancibia-Avila, P., Toledo-Montiel, F., Paśko, P., & Gorinstein, S. (2026). Molecular Interactions and Antioxidant Properties of White Wine Phytochemicals: A Mechanistic Study of Serum Protein Binding. Biomolecules, 16(8), 1153. https://doi.org/10.3390/biom16081153

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