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Title: | β-lactoglobulin conformation influences its interaction with caffeine |
Keywords: | Bioactive compounds Protein thermodynamic binding Isothermal titration calorimetry Molecular docking Compostos bioativos Ligação termodinâmica de proteínas Calorimetria de titulação isotérmica |
Publisher: | Elsevier |
Citation: | ROSA, L. N. S. et al. β-lactoglobulin conformation influences its interaction with caffeine. Food Bioscience, [S. l.], v. 44, 101418, Dec. 2021. Part A. DOI: 10.1016/j.fbio.2021.101418. |
Abstract: | Caffeine is a molecule with bioactive properties related to increased mental performance. Its use in food products is limited by its bitterness and self-association behavior. The complex formed by β-lactoglobulin and caffeine was characterized by fluorescence spectroscopy, isothermal titration calorimetry, and molecular docking. Fluorescence spectroscopy revealed that β-lactoglobulin interacted with caffeine to form a 1:1 stoichiometric complex. Isothermal titration calorimetry characterization of β-lactoglobulin-caffeine binding revealed a different stoichiometry (1:3). Molecular docking analysis confirmed the information obtained by the two thermodynamic evaluation techniques, showing that the best interaction occurred in the hydrophobic cavity of β-lactoglobulin. The effect of protein conformation was also evaluated by fluorescence spectroscopy. The complex stoichiometry and binding constants were from the same order as those obtained for native β-lactoglobulin. However, in contrast to the complex formation with native protein, the flexibility increase observed in the thermal unfolded protein promoted a great temperature effect on the standard enthalpy and entropy changes of interaction, indicating the presence of a balance between hydrophobic and hydrophilic forces. |
URI: | https://doi.org/10.1016/j.fbio.2021.101418 http://repositorio.ufla.br/jspui/handle/1/50785 |
Appears in Collections: | DCA - Artigos publicados em periódicos |
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