Academic Journal
Fluorescence spectroscopy, 3D-QSAR, and molecular dynamics analyses reveal the interaction mechanisms of flavonoids with lysozyme.
| Τίτλος: | Fluorescence spectroscopy, 3D-QSAR, and molecular dynamics analyses reveal the interaction mechanisms of flavonoids with lysozyme. |
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| Συγγραφείς: | Geng S; School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China; Henan Advanced Agriculture and Future Foods Research Association, Zhengzhou 450046, China., Liu G; School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China., Bai L; School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China., Wang C; School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China., Yang W; School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China., Jia Y; School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China., Liu H; School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China., Liu B; School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China. Electronic address: liubenguo@hist.edu.cn. |
| Πηγή: | Food chemistry [Food Chem] 2026 Aug 15; Vol. 520, pp. 149859. Date of Electronic Publication: 2026 May 28. |
| Τύπος έκδοσης: | Journal Article |
| Γλώσσα: | English |
| Στοιχεία περιοδικού: | Publisher: Elsevier Applied Science Publishers Country of Publication: England NLM ID: 7702639 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-7072 (Electronic) Linking ISSN: 03088146 NLM ISO Abbreviation: Food Chem Subsets: MEDLINE |
| Imprint Name(s): | Publication: Barking : Elsevier Applied Science Publishers Original Publication: Barking, Eng., Applied Science Publishers. |
| Ιατρικοί όροι (MeSH): | Flavonoids*/chemistry , Muramidase*/chemistry, Quantitative Structure-Activity Relationship ; Molecular Dynamics Simulation ; Spectrometry, Fluorescence ; Hydrogen Bonding ; Protein Binding ; Hydrophobic and Hydrophilic Interactions ; Animals ; Molecular Structure |
| Περίληψη: | This research elucidates the mechanisms of non-covalent interactions between flavonoids and lysozyme. Binding constants were determined via fluorescence spectroscopy, and a Topomer CoMFA 3D-QSAR model was developed, effectively explaining the binding behavior. Detailed studies on rutin, naringenin, and hesperetin showed binding occurred via a static quenching mechanism with a 1:1 stoichiometry, and hydrogen bonding and van der Waals forces were indicated as the primary drivers. Synchronous fluorescence revealed flavonoid binding disrupted the tryptophan microenvironment but left tyrosine relatively stable. IGM analysis of rutin glycosylation revealed a rigid intramolecular hydrogen-bond network, whereas the aglycones were less stable. Intermolecularly, rutin formed multiple hydrogen bonds and extensive hydrophobic interactions, while aglycone binding was simpler. MD simulations and free energy calculations yielded the following binding affinity: hesperetin > naringenin > rutin, underscoring the importance of solvation effects. This work provides molecular-level insights into the structure-activity relationship, aiding the design of flavonoid delivery systems. (Copyright © 2026 Elsevier Ltd. All rights reserved.) |
| Competing Interests: | Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. |
| Contributed Indexing: | Keywords: 3D-QSAR; Flavonoids; Fluorescence spectroscopy; Lysozyme; Molecular simulation |
| Substance Nomenclature: | 0 (Flavonoids) EC 3.2.1.17 (Muramidase) |
| Entry Date(s): | Date Created: 20260531 Date Completed: 20260613 Latest Revision: 20260613 |
| Update Code: | 20260613 |
| DOI: | 10.1016/j.foodchem.2026.149859 |
| PMID: | 42218868 |
| Βάση Δεδομένων: | MEDLINE |
| ISSN: | 1873-7072 |
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| DOI: | 10.1016/j.foodchem.2026.149859 |