Fluorescence spectroscopy and molecular modeling of anthocyanins binding to bovine lactoferrin peptides

•The anthocyanins-binding capabilities of lactoferrin peptides were tested.•20 peptides were identified, from which four contained Trp at C-terminal.•van der Waals and hydrogen bonding are responsible for anthocyanins binding.•Trp containing peptides bind delphynidine-3-glycoside or delphynidine-3-rutinoside.•New ingredients with enhanced properties were provided. This work was aimed to obtain lactoferrin peptides, with anthocyanins-binding capabilities, by using eggplant peels extract as a source of anthocyanins. The chromatographic analysis of the extract evidenced the presence of five individual anthocyanins, with delfinidin-3-rutinoside being identified as the predominant. 20 small peptides were identified, from which four are containing Trp at C-terminal. By estimating the thermodynamic parameters, van der Waals and hydrogen bonding were found to have important roles in binding of anthocyanins to LF and LF-derived peptides. In order to complement the experimental results, the in silico methods were further employed to add single molecule level details on the potential interactions between different peptides and the main anthocyanins from eggplant peels. The docking tests indicated that the Trp containing peptides can bind, with different affinities either delphynidine-3-glycoside or delphynidine-3-rutinoside, therefore explaining the fluorescence quenching results. Our results have indicated a mechanism for the interactions between anthocyanins and LF and its small molecular weight peptides, whereas providing insights for formulating ingredients and foods with enhanced bioactives-binding properties.