Dinu, V., Borah, P.K., Muleya, M. et al. (6 more authors) (2022) Flavour compounds affect protein structure: The effect of methyl anthranilate on bovine serum albumin conformation. Food Chemistry, 388. 133013. ISSN 0308-8146
Abstract
This study aims to understand possible effects of flavour compounds on the structure and conformation of endogenous proteins. Using methyl anthranilate (a grape flavour compound added to drinks, confectionery, and vape-liquids) and bovine serum albumin (BSA, a model serum protein) we designed experimental investigations using analytical ultracentrifugation, size exclusion chromatography small angle X-ray scattering, and fluorescence spectroscopy to reveal that methyl anthranilate spontaneously binds to BSA (ΔG°, ca. −21 KJ mol−1) which induces a conformational compactness (ca. 10 %) in the monomer structure. Complementary molecular modelling and dynamics simulations suggested the binding occurs at Sudlow II of BSA via establishment of hydrogen bonds with arginine409, lysine413 and serine488 leading to an increased conformational order in domains IA, IIB and IIIB. This work aims to set the foundation for future research on flavour-protein interactions and offer new sets of opportunities for understanding the effects of small compounds on protein structure.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Keywords: | Bovine serum albumin; Methyl anthranilate; Flavour; Structure; AUC; SAXS |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Environment (Leeds) > School of Food Science and Nutrition (Leeds) > FSN Chemistry and Biochemistry (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 29 Jan 2025 13:41 |
Last Modified: | 29 Jan 2025 13:41 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.foodchem.2022.133013 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:222525 |