Flavour compounds affect protein structure: the effect of methyl anthranilate on bovine serum albumin conformation

Dinu, Vlad, Borah, Borah P, Muleya, Molly, Scott, David J, Lithgo, Ryan, Pattem, Jacob ORCID: https://orcid.org/0000-0003-0276-7996, Harding, Stephen E., Yakubov, Gleb E. and Fisk, Ian D. 2022. Flavour compounds affect protein structure: the effect of methyl anthranilate on bovine serum albumin conformation. Food Chemistry 388 , 133013. 10.1016/j.foodchem.2022.133013

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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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Publisher:	Elsevier
ISSN:	0308-8146
Date of Acceptance:	17 April 2022
Last Modified:	24 Oct 2023 12:45
URI:	https://orca.cardiff.ac.uk/id/eprint/162535

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