Abstract
Interactions and binding mechanisms between soybean glycinin (11S) and genistein were investigated at near neutral pH (7.4) and ambient temperature using various spectroscopic techniques and molecular docking. Ultra-violet visible spectroscopy revealed non-covalent bonds were responsible for the stabilisation of the complex. Following complexation, minor reductions in the alpha helix and beta sheet content of the protein were confirmed by circular dichroism (CD) and infrared spectroscopy (FTIR). Fluorescence quenching and molecular docking predicted a 11S trimer and genistein complex with a 1:1 stoichiometric ratio, with the binding location predominantly on the interior portion of the protein, stabilised in majority by hydrogen bonds. Although binding was determined to be of moderate strength, secondary structure characterisation suggested that the structural components of the protein remained largely unchanged. This outcome indicates that the ligand can be accommodated in the interior of the 11S trimer, forming a stable complex within the present conditions of neutral pH and ambient temperature.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
